data_8Z35
# 
_entry.id   8Z35 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   8Z35         pdb_00008z35 10.2210/pdb8z35/pdb 
WWPDB D_1300046933 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-02-26 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8Z35 
_pdbx_database_status.recvd_initial_deposition_date   2024-04-14 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.details 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
PDB . 8Z31 unspecified 
PDB . 8Z32 unspecified 
PDB . 8Z33 unspecified 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              shuichiro.ito@daiichisankyo.com 
_pdbx_contact_author.name_first         Shuichiro 
_pdbx_contact_author.name_last          Ito 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-6314-2503 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Ito, S.'    1 0000-0002-6314-2503 
'Baba, D.'   2 ?                   
'Fukuda, T.' 3 ?                   
'Tanaka, N.' 4 ?                   
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Bioorg.Med.Chem.Lett. 
_citation.journal_id_ASTM           BMCLE8 
_citation.journal_id_CSD            1127 
_citation.journal_id_ISSN           1464-3405 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            108 
_citation.language                  ? 
_citation.page_first                129799 
_citation.page_last                 129799 
_citation.title                     
'Discovery of DS44470011: An oral hypoxia-inducible factor prolyl hydroxylase inhibitor for the treatment of renal anemia.' 
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.bmcl.2024.129799 
_citation.pdbx_database_id_PubMed   38754564 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Fukuda, T.'      1  ? 
primary 'Kuribayashi, T.' 2  ? 
primary 'Takano, R.'      3  ? 
primary 'Sasaki, K.'      4  ? 
primary 'Tsuji, T.'       5  ? 
primary 'Niitsu, Y.'      6  ? 
primary 'Ishii, K.'       7  ? 
primary 'Hashimoto, M.'   8  ? 
primary 'Baba, D.'        9  ? 
primary 'Ito, S.'         10 ? 
primary 'Tanaka, N.'      11 ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Egl nine homolog 1'                                                                           25371.887 1   
1.14.11.29 ? ? ? 
2 non-polymer syn 'FE (II) ION'                                                                                  55.845    1   ? ? 
? ? 
3 non-polymer syn 'SULFATE ION'                                                                                  96.063    2   ? ? 
? ? 
4 non-polymer syn 'CHLORIDE ION'                                                                                 35.453    1   ? ? 
? ? 
5 non-polymer nat '2-[[6-methyl-5-oxidanyl-2-[(4-phenylphenyl)methyl]pyrimidin-4-yl]carbonylamino]ethanoic acid' 377.393   1   ? ? 
? ? 
6 water       nat water                                                                                          18.015    112 ? ? 
? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        
;Hypoxia-inducible factor prolyl hydroxylase 2,HIF-PH2,HIF-prolyl hydroxylase 2,HPH-2,Prolyl hydroxylase domain-containing protein 2,PHD2,SM-20
;
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MAHHHHHHLPALKLALEYIVPCMNKHGICVVDDFLGKETGQQIGDEVRALHDTGKFTDGQLVSQKSDSSKDIRGDKITWI
EGKEPGCETIGLLMSSMDDLIRHCNGKLGSYKINGRTKAMVACYPGNGTGYVRHVDNPNGDGRCVTCIYYLNKDWDAKVS
GGILRIFPEGKAQFADIEPKFDRLLFFWSDRRNPHEVQPAYATRYAITVWYFDADERARAKVKY
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MAHHHHHHLPALKLALEYIVPCMNKHGICVVDDFLGKETGQQIGDEVRALHDTGKFTDGQLVSQKSDSSKDIRGDKITWI
EGKEPGCETIGLLMSSMDDLIRHCNGKLGSYKINGRTKAMVACYPGNGTGYVRHVDNPNGDGRCVTCIYYLNKDWDAKVS
GGILRIFPEGKAQFADIEPKFDRLLFFWSDRRNPHEVQPAYATRYAITVWYFDADERARAKVKY
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'FE (II) ION'                                                                                  FE2   
3 'SULFATE ION'                                                                                  SO4   
4 'CHLORIDE ION'                                                                                 CL    
5 '2-[[6-methyl-5-oxidanyl-2-[(4-phenylphenyl)methyl]pyrimidin-4-yl]carbonylamino]ethanoic acid' A1L0X 
6 water                                                                                          HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   ALA n 
1 3   HIS n 
1 4   HIS n 
1 5   HIS n 
1 6   HIS n 
1 7   HIS n 
1 8   HIS n 
1 9   LEU n 
1 10  PRO n 
1 11  ALA n 
1 12  LEU n 
1 13  LYS n 
1 14  LEU n 
1 15  ALA n 
1 16  LEU n 
1 17  GLU n 
1 18  TYR n 
1 19  ILE n 
1 20  VAL n 
1 21  PRO n 
1 22  CYS n 
1 23  MET n 
1 24  ASN n 
1 25  LYS n 
1 26  HIS n 
1 27  GLY n 
1 28  ILE n 
1 29  CYS n 
1 30  VAL n 
1 31  VAL n 
1 32  ASP n 
1 33  ASP n 
1 34  PHE n 
1 35  LEU n 
1 36  GLY n 
1 37  LYS n 
1 38  GLU n 
1 39  THR n 
1 40  GLY n 
1 41  GLN n 
1 42  GLN n 
1 43  ILE n 
1 44  GLY n 
1 45  ASP n 
1 46  GLU n 
1 47  VAL n 
1 48  ARG n 
1 49  ALA n 
1 50  LEU n 
1 51  HIS n 
1 52  ASP n 
1 53  THR n 
1 54  GLY n 
1 55  LYS n 
1 56  PHE n 
1 57  THR n 
1 58  ASP n 
1 59  GLY n 
1 60  GLN n 
1 61  LEU n 
1 62  VAL n 
1 63  SER n 
1 64  GLN n 
1 65  LYS n 
1 66  SER n 
1 67  ASP n 
1 68  SER n 
1 69  SER n 
1 70  LYS n 
1 71  ASP n 
1 72  ILE n 
1 73  ARG n 
1 74  GLY n 
1 75  ASP n 
1 76  LYS n 
1 77  ILE n 
1 78  THR n 
1 79  TRP n 
1 80  ILE n 
1 81  GLU n 
1 82  GLY n 
1 83  LYS n 
1 84  GLU n 
1 85  PRO n 
1 86  GLY n 
1 87  CYS n 
1 88  GLU n 
1 89  THR n 
1 90  ILE n 
1 91  GLY n 
1 92  LEU n 
1 93  LEU n 
1 94  MET n 
1 95  SER n 
1 96  SER n 
1 97  MET n 
1 98  ASP n 
1 99  ASP n 
1 100 LEU n 
1 101 ILE n 
1 102 ARG n 
1 103 HIS n 
1 104 CYS n 
1 105 ASN n 
1 106 GLY n 
1 107 LYS n 
1 108 LEU n 
1 109 GLY n 
1 110 SER n 
1 111 TYR n 
1 112 LYS n 
1 113 ILE n 
1 114 ASN n 
1 115 GLY n 
1 116 ARG n 
1 117 THR n 
1 118 LYS n 
1 119 ALA n 
1 120 MET n 
1 121 VAL n 
1 122 ALA n 
1 123 CYS n 
1 124 TYR n 
1 125 PRO n 
1 126 GLY n 
1 127 ASN n 
1 128 GLY n 
1 129 THR n 
1 130 GLY n 
1 131 TYR n 
1 132 VAL n 
1 133 ARG n 
1 134 HIS n 
1 135 VAL n 
1 136 ASP n 
1 137 ASN n 
1 138 PRO n 
1 139 ASN n 
1 140 GLY n 
1 141 ASP n 
1 142 GLY n 
1 143 ARG n 
1 144 CYS n 
1 145 VAL n 
1 146 THR n 
1 147 CYS n 
1 148 ILE n 
1 149 TYR n 
1 150 TYR n 
1 151 LEU n 
1 152 ASN n 
1 153 LYS n 
1 154 ASP n 
1 155 TRP n 
1 156 ASP n 
1 157 ALA n 
1 158 LYS n 
1 159 VAL n 
1 160 SER n 
1 161 GLY n 
1 162 GLY n 
1 163 ILE n 
1 164 LEU n 
1 165 ARG n 
1 166 ILE n 
1 167 PHE n 
1 168 PRO n 
1 169 GLU n 
1 170 GLY n 
1 171 LYS n 
1 172 ALA n 
1 173 GLN n 
1 174 PHE n 
1 175 ALA n 
1 176 ASP n 
1 177 ILE n 
1 178 GLU n 
1 179 PRO n 
1 180 LYS n 
1 181 PHE n 
1 182 ASP n 
1 183 ARG n 
1 184 LEU n 
1 185 LEU n 
1 186 PHE n 
1 187 PHE n 
1 188 TRP n 
1 189 SER n 
1 190 ASP n 
1 191 ARG n 
1 192 ARG n 
1 193 ASN n 
1 194 PRO n 
1 195 HIS n 
1 196 GLU n 
1 197 VAL n 
1 198 GLN n 
1 199 PRO n 
1 200 ALA n 
1 201 TYR n 
1 202 ALA n 
1 203 THR n 
1 204 ARG n 
1 205 TYR n 
1 206 ALA n 
1 207 ILE n 
1 208 THR n 
1 209 VAL n 
1 210 TRP n 
1 211 TYR n 
1 212 PHE n 
1 213 ASP n 
1 214 ALA n 
1 215 ASP n 
1 216 GLU n 
1 217 ARG n 
1 218 ALA n 
1 219 ARG n 
1 220 ALA n 
1 221 LYS n 
1 222 VAL n 
1 223 LYS n 
1 224 TYR n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   224 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'EGLN1, C1orf12, PNAS-118, PNAS-137' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          pDEST14 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1L0X non-polymer         . '2-[[6-methyl-5-oxidanyl-2-[(4-phenylphenyl)methyl]pyrimidin-4-yl]carbonylamino]ethanoic acid' ? 
'C21 H19 N3 O4'  377.393 
ALA   'L-peptide linking' y ALANINE                                                                                        ? 
'C3 H7 N O2'     89.093  
ARG   'L-peptide linking' y ARGININE                                                                                       ? 
'C6 H15 N4 O2 1' 175.209 
ASN   'L-peptide linking' y ASPARAGINE                                                                                     ? 
'C4 H8 N2 O3'    132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                                                                ? 
'C4 H7 N O4'     133.103 
CL    non-polymer         . 'CHLORIDE ION'                                                                                 ? 
'Cl -1'          35.453  
CYS   'L-peptide linking' y CYSTEINE                                                                                       ? 
'C3 H7 N O2 S'   121.158 
FE2   non-polymer         . 'FE (II) ION'                                                                                  ? 
'Fe 2'           55.845  
GLN   'L-peptide linking' y GLUTAMINE                                                                                      ? 
'C5 H10 N2 O3'   146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                                                ? 
'C5 H9 N O4'     147.129 
GLY   'peptide linking'   y GLYCINE                                                                                        ? 
'C2 H5 N O2'     75.067  
HIS   'L-peptide linking' y HISTIDINE                                                                                      ? 
'C6 H10 N3 O2 1' 156.162 
HOH   non-polymer         . WATER                                                                                          ? 
'H2 O'           18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                                                     ? 
'C6 H13 N O2'    131.173 
LEU   'L-peptide linking' y LEUCINE                                                                                        ? 
'C6 H13 N O2'    131.173 
LYS   'L-peptide linking' y LYSINE                                                                                         ? 
'C6 H15 N2 O2 1' 147.195 
MET   'L-peptide linking' y METHIONINE                                                                                     ? 
'C5 H11 N O2 S'  149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                                                                  ? 
'C9 H11 N O2'    165.189 
PRO   'L-peptide linking' y PROLINE                                                                                        ? 
'C5 H9 N O2'     115.130 
SER   'L-peptide linking' y SERINE                                                                                         ? 
'C3 H7 N O3'     105.093 
SO4   non-polymer         . 'SULFATE ION'                                                                                  ? 
'O4 S -2'        96.063  
THR   'L-peptide linking' y THREONINE                                                                                      ? 
'C4 H9 N O3'     119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                                                                     ? 
'C11 H12 N2 O2'  204.225 
TYR   'L-peptide linking' y TYROSINE                                                                                       ? 
'C9 H11 N O3'    181.189 
VAL   'L-peptide linking' y VALINE                                                                                         ? 
'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   180 ?   ?   ?   A . n 
A 1 2   ALA 2   181 ?   ?   ?   A . n 
A 1 3   HIS 3   182 182 HIS HIS A . n 
A 1 4   HIS 4   183 183 HIS HIS A . n 
A 1 5   HIS 5   184 184 HIS HIS A . n 
A 1 6   HIS 6   185 185 HIS HIS A . n 
A 1 7   HIS 7   186 186 HIS HIS A . n 
A 1 8   HIS 8   187 187 HIS HIS A . n 
A 1 9   LEU 9   188 188 LEU LEU A . n 
A 1 10  PRO 10  189 189 PRO PRO A . n 
A 1 11  ALA 11  190 190 ALA ALA A . n 
A 1 12  LEU 12  191 191 LEU LEU A . n 
A 1 13  LYS 13  192 192 LYS LYS A . n 
A 1 14  LEU 14  193 193 LEU LEU A . n 
A 1 15  ALA 15  194 194 ALA ALA A . n 
A 1 16  LEU 16  195 195 LEU LEU A . n 
A 1 17  GLU 17  196 196 GLU GLU A . n 
A 1 18  TYR 18  197 197 TYR TYR A . n 
A 1 19  ILE 19  198 198 ILE ILE A . n 
A 1 20  VAL 20  199 199 VAL VAL A . n 
A 1 21  PRO 21  200 200 PRO PRO A . n 
A 1 22  CYS 22  201 201 CYS CYS A . n 
A 1 23  MET 23  202 202 MET MET A . n 
A 1 24  ASN 24  203 203 ASN ASN A . n 
A 1 25  LYS 25  204 204 LYS LYS A . n 
A 1 26  HIS 26  205 205 HIS HIS A . n 
A 1 27  GLY 27  206 206 GLY GLY A . n 
A 1 28  ILE 28  207 207 ILE ILE A . n 
A 1 29  CYS 29  208 208 CYS CYS A . n 
A 1 30  VAL 30  209 209 VAL VAL A . n 
A 1 31  VAL 31  210 210 VAL VAL A . n 
A 1 32  ASP 32  211 211 ASP ASP A . n 
A 1 33  ASP 33  212 212 ASP ASP A . n 
A 1 34  PHE 34  213 213 PHE PHE A . n 
A 1 35  LEU 35  214 214 LEU LEU A . n 
A 1 36  GLY 36  215 215 GLY GLY A . n 
A 1 37  LYS 37  216 216 LYS LYS A . n 
A 1 38  GLU 38  217 217 GLU GLU A . n 
A 1 39  THR 39  218 218 THR THR A . n 
A 1 40  GLY 40  219 219 GLY GLY A . n 
A 1 41  GLN 41  220 220 GLN GLN A . n 
A 1 42  GLN 42  221 221 GLN GLN A . n 
A 1 43  ILE 43  222 222 ILE ILE A . n 
A 1 44  GLY 44  223 223 GLY GLY A . n 
A 1 45  ASP 45  224 224 ASP ASP A . n 
A 1 46  GLU 46  225 225 GLU GLU A . n 
A 1 47  VAL 47  226 226 VAL VAL A . n 
A 1 48  ARG 48  227 227 ARG ARG A . n 
A 1 49  ALA 49  228 228 ALA ALA A . n 
A 1 50  LEU 50  229 229 LEU LEU A . n 
A 1 51  HIS 51  230 230 HIS HIS A . n 
A 1 52  ASP 52  231 231 ASP ASP A . n 
A 1 53  THR 53  232 232 THR THR A . n 
A 1 54  GLY 54  233 233 GLY GLY A . n 
A 1 55  LYS 55  234 234 LYS LYS A . n 
A 1 56  PHE 56  235 235 PHE PHE A . n 
A 1 57  THR 57  236 236 THR THR A . n 
A 1 58  ASP 58  237 237 ASP ASP A . n 
A 1 59  GLY 59  238 238 GLY GLY A . n 
A 1 60  GLN 60  239 239 GLN GLN A . n 
A 1 61  LEU 61  240 240 LEU LEU A . n 
A 1 62  VAL 62  241 241 VAL VAL A . n 
A 1 63  SER 63  242 242 SER SER A . n 
A 1 64  GLN 64  243 ?   ?   ?   A . n 
A 1 65  LYS 65  244 ?   ?   ?   A . n 
A 1 66  SER 66  245 ?   ?   ?   A . n 
A 1 67  ASP 67  246 ?   ?   ?   A . n 
A 1 68  SER 68  247 ?   ?   ?   A . n 
A 1 69  SER 69  248 ?   ?   ?   A . n 
A 1 70  LYS 70  249 ?   ?   ?   A . n 
A 1 71  ASP 71  250 250 ASP ASP A . n 
A 1 72  ILE 72  251 251 ILE ILE A . n 
A 1 73  ARG 73  252 252 ARG ARG A . n 
A 1 74  GLY 74  253 253 GLY GLY A . n 
A 1 75  ASP 75  254 254 ASP ASP A . n 
A 1 76  LYS 76  255 255 LYS LYS A . n 
A 1 77  ILE 77  256 256 ILE ILE A . n 
A 1 78  THR 78  257 257 THR THR A . n 
A 1 79  TRP 79  258 258 TRP TRP A . n 
A 1 80  ILE 80  259 259 ILE ILE A . n 
A 1 81  GLU 81  260 260 GLU GLU A . n 
A 1 82  GLY 82  261 261 GLY GLY A . n 
A 1 83  LYS 83  262 262 LYS LYS A . n 
A 1 84  GLU 84  263 263 GLU GLU A . n 
A 1 85  PRO 85  264 264 PRO PRO A . n 
A 1 86  GLY 86  265 265 GLY GLY A . n 
A 1 87  CYS 87  266 266 CYS CYS A . n 
A 1 88  GLU 88  267 267 GLU GLU A . n 
A 1 89  THR 89  268 268 THR THR A . n 
A 1 90  ILE 90  269 269 ILE ILE A . n 
A 1 91  GLY 91  270 270 GLY GLY A . n 
A 1 92  LEU 92  271 271 LEU LEU A . n 
A 1 93  LEU 93  272 272 LEU LEU A . n 
A 1 94  MET 94  273 273 MET MET A . n 
A 1 95  SER 95  274 274 SER SER A . n 
A 1 96  SER 96  275 275 SER SER A . n 
A 1 97  MET 97  276 276 MET MET A . n 
A 1 98  ASP 98  277 277 ASP ASP A . n 
A 1 99  ASP 99  278 278 ASP ASP A . n 
A 1 100 LEU 100 279 279 LEU LEU A . n 
A 1 101 ILE 101 280 280 ILE ILE A . n 
A 1 102 ARG 102 281 281 ARG ARG A . n 
A 1 103 HIS 103 282 282 HIS HIS A . n 
A 1 104 CYS 104 283 283 CYS CYS A . n 
A 1 105 ASN 105 284 284 ASN ASN A . n 
A 1 106 GLY 106 285 285 GLY GLY A . n 
A 1 107 LYS 107 286 286 LYS LYS A . n 
A 1 108 LEU 108 287 287 LEU LEU A . n 
A 1 109 GLY 109 288 288 GLY GLY A . n 
A 1 110 SER 110 289 289 SER SER A . n 
A 1 111 TYR 111 290 290 TYR TYR A . n 
A 1 112 LYS 112 291 291 LYS LYS A . n 
A 1 113 ILE 113 292 292 ILE ILE A . n 
A 1 114 ASN 114 293 293 ASN ASN A . n 
A 1 115 GLY 115 294 294 GLY GLY A . n 
A 1 116 ARG 116 295 295 ARG ARG A . n 
A 1 117 THR 117 296 296 THR THR A . n 
A 1 118 LYS 118 297 297 LYS LYS A . n 
A 1 119 ALA 119 298 298 ALA ALA A . n 
A 1 120 MET 120 299 299 MET MET A . n 
A 1 121 VAL 121 300 300 VAL VAL A . n 
A 1 122 ALA 122 301 301 ALA ALA A . n 
A 1 123 CYS 123 302 302 CYS CYS A . n 
A 1 124 TYR 124 303 303 TYR TYR A . n 
A 1 125 PRO 125 304 304 PRO PRO A . n 
A 1 126 GLY 126 305 305 GLY GLY A . n 
A 1 127 ASN 127 306 306 ASN ASN A . n 
A 1 128 GLY 128 307 307 GLY GLY A . n 
A 1 129 THR 129 308 308 THR THR A . n 
A 1 130 GLY 130 309 309 GLY GLY A . n 
A 1 131 TYR 131 310 310 TYR TYR A . n 
A 1 132 VAL 132 311 311 VAL VAL A . n 
A 1 133 ARG 133 312 312 ARG ARG A . n 
A 1 134 HIS 134 313 313 HIS HIS A . n 
A 1 135 VAL 135 314 314 VAL VAL A . n 
A 1 136 ASP 136 315 315 ASP ASP A . n 
A 1 137 ASN 137 316 316 ASN ASN A . n 
A 1 138 PRO 138 317 317 PRO PRO A . n 
A 1 139 ASN 139 318 318 ASN ASN A . n 
A 1 140 GLY 140 319 319 GLY GLY A . n 
A 1 141 ASP 141 320 320 ASP ASP A . n 
A 1 142 GLY 142 321 321 GLY GLY A . n 
A 1 143 ARG 143 322 322 ARG ARG A . n 
A 1 144 CYS 144 323 323 CYS CYS A . n 
A 1 145 VAL 145 324 324 VAL VAL A . n 
A 1 146 THR 146 325 325 THR THR A . n 
A 1 147 CYS 147 326 326 CYS CYS A . n 
A 1 148 ILE 148 327 327 ILE ILE A . n 
A 1 149 TYR 149 328 328 TYR TYR A . n 
A 1 150 TYR 150 329 329 TYR TYR A . n 
A 1 151 LEU 151 330 330 LEU LEU A . n 
A 1 152 ASN 152 331 331 ASN ASN A . n 
A 1 153 LYS 153 332 332 LYS LYS A . n 
A 1 154 ASP 154 333 333 ASP ASP A . n 
A 1 155 TRP 155 334 334 TRP TRP A . n 
A 1 156 ASP 156 335 335 ASP ASP A . n 
A 1 157 ALA 157 336 336 ALA ALA A . n 
A 1 158 LYS 158 337 337 LYS LYS A . n 
A 1 159 VAL 159 338 338 VAL VAL A . n 
A 1 160 SER 160 339 339 SER SER A . n 
A 1 161 GLY 161 340 340 GLY GLY A . n 
A 1 162 GLY 162 341 341 GLY GLY A . n 
A 1 163 ILE 163 342 342 ILE ILE A . n 
A 1 164 LEU 164 343 343 LEU LEU A . n 
A 1 165 ARG 165 344 344 ARG ARG A . n 
A 1 166 ILE 166 345 345 ILE ILE A . n 
A 1 167 PHE 167 346 346 PHE PHE A . n 
A 1 168 PRO 168 347 347 PRO PRO A . n 
A 1 169 GLU 169 348 348 GLU GLU A . n 
A 1 170 GLY 170 349 349 GLY GLY A . n 
A 1 171 LYS 171 350 350 LYS LYS A . n 
A 1 172 ALA 172 351 351 ALA ALA A . n 
A 1 173 GLN 173 352 352 GLN GLN A . n 
A 1 174 PHE 174 353 353 PHE PHE A . n 
A 1 175 ALA 175 354 354 ALA ALA A . n 
A 1 176 ASP 176 355 355 ASP ASP A . n 
A 1 177 ILE 177 356 356 ILE ILE A . n 
A 1 178 GLU 178 357 357 GLU GLU A . n 
A 1 179 PRO 179 358 358 PRO PRO A . n 
A 1 180 LYS 180 359 359 LYS LYS A . n 
A 1 181 PHE 181 360 360 PHE PHE A . n 
A 1 182 ASP 182 361 361 ASP ASP A . n 
A 1 183 ARG 183 362 362 ARG ARG A . n 
A 1 184 LEU 184 363 363 LEU LEU A . n 
A 1 185 LEU 185 364 364 LEU LEU A . n 
A 1 186 PHE 186 365 365 PHE PHE A . n 
A 1 187 PHE 187 366 366 PHE PHE A . n 
A 1 188 TRP 188 367 367 TRP TRP A . n 
A 1 189 SER 189 368 368 SER SER A . n 
A 1 190 ASP 190 369 369 ASP ASP A . n 
A 1 191 ARG 191 370 370 ARG ARG A . n 
A 1 192 ARG 192 371 371 ARG ARG A . n 
A 1 193 ASN 193 372 372 ASN ASN A . n 
A 1 194 PRO 194 373 373 PRO PRO A . n 
A 1 195 HIS 195 374 374 HIS HIS A . n 
A 1 196 GLU 196 375 375 GLU GLU A . n 
A 1 197 VAL 197 376 376 VAL VAL A . n 
A 1 198 GLN 198 377 377 GLN GLN A . n 
A 1 199 PRO 199 378 378 PRO PRO A . n 
A 1 200 ALA 200 379 379 ALA ALA A . n 
A 1 201 TYR 201 380 380 TYR TYR A . n 
A 1 202 ALA 202 381 381 ALA ALA A . n 
A 1 203 THR 203 382 382 THR THR A . n 
A 1 204 ARG 204 383 383 ARG ARG A . n 
A 1 205 TYR 205 384 384 TYR TYR A . n 
A 1 206 ALA 206 385 385 ALA ALA A . n 
A 1 207 ILE 207 386 386 ILE ILE A . n 
A 1 208 THR 208 387 387 THR THR A . n 
A 1 209 VAL 209 388 388 VAL VAL A . n 
A 1 210 TRP 210 389 389 TRP TRP A . n 
A 1 211 TYR 211 390 390 TYR TYR A . n 
A 1 212 PHE 212 391 391 PHE PHE A . n 
A 1 213 ASP 213 392 392 ASP ASP A . n 
A 1 214 ALA 214 393 393 ALA ALA A . n 
A 1 215 ASP 215 394 394 ASP ASP A . n 
A 1 216 GLU 216 395 395 GLU GLU A . n 
A 1 217 ARG 217 396 396 ARG ARG A . n 
A 1 218 ALA 218 397 397 ALA ALA A . n 
A 1 219 ARG 219 398 398 ARG ARG A . n 
A 1 220 ALA 220 399 399 ALA ALA A . n 
A 1 221 LYS 221 400 400 LYS LYS A . n 
A 1 222 VAL 222 401 401 VAL VAL A . n 
A 1 223 LYS 223 402 402 LYS LYS A . n 
A 1 224 TYR 224 403 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1L0X 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1L0X 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 FE2   1   501 1   FE2   FE2 A . 
C 3 SO4   1   502 1   SO4   SO4 A . 
D 3 SO4   1   503 2   SO4   SO4 A . 
E 4 CL    1   504 1   CL    CL  A . 
F 5 A1L0X 1   505 1   A1L0X IN7 A . 
G 6 HOH   1   601 87  HOH   HOH A . 
G 6 HOH   2   602 13  HOH   HOH A . 
G 6 HOH   3   603 8   HOH   HOH A . 
G 6 HOH   4   604 93  HOH   HOH A . 
G 6 HOH   5   605 11  HOH   HOH A . 
G 6 HOH   6   606 17  HOH   HOH A . 
G 6 HOH   7   607 18  HOH   HOH A . 
G 6 HOH   8   608 52  HOH   HOH A . 
G 6 HOH   9   609 16  HOH   HOH A . 
G 6 HOH   10  610 2   HOH   HOH A . 
G 6 HOH   11  611 67  HOH   HOH A . 
G 6 HOH   12  612 40  HOH   HOH A . 
G 6 HOH   13  613 6   HOH   HOH A . 
G 6 HOH   14  614 69  HOH   HOH A . 
G 6 HOH   15  615 31  HOH   HOH A . 
G 6 HOH   16  616 39  HOH   HOH A . 
G 6 HOH   17  617 71  HOH   HOH A . 
G 6 HOH   18  618 23  HOH   HOH A . 
G 6 HOH   19  619 77  HOH   HOH A . 
G 6 HOH   20  620 4   HOH   HOH A . 
G 6 HOH   21  621 53  HOH   HOH A . 
G 6 HOH   22  622 96  HOH   HOH A . 
G 6 HOH   23  623 102 HOH   HOH A . 
G 6 HOH   24  624 10  HOH   HOH A . 
G 6 HOH   25  625 92  HOH   HOH A . 
G 6 HOH   26  626 7   HOH   HOH A . 
G 6 HOH   27  627 30  HOH   HOH A . 
G 6 HOH   28  628 26  HOH   HOH A . 
G 6 HOH   29  629 34  HOH   HOH A . 
G 6 HOH   30  630 38  HOH   HOH A . 
G 6 HOH   31  631 3   HOH   HOH A . 
G 6 HOH   32  632 108 HOH   HOH A . 
G 6 HOH   33  633 74  HOH   HOH A . 
G 6 HOH   34  634 47  HOH   HOH A . 
G 6 HOH   35  635 5   HOH   HOH A . 
G 6 HOH   36  636 36  HOH   HOH A . 
G 6 HOH   37  637 24  HOH   HOH A . 
G 6 HOH   38  638 28  HOH   HOH A . 
G 6 HOH   39  639 27  HOH   HOH A . 
G 6 HOH   40  640 1   HOH   HOH A . 
G 6 HOH   41  641 33  HOH   HOH A . 
G 6 HOH   42  642 68  HOH   HOH A . 
G 6 HOH   43  643 21  HOH   HOH A . 
G 6 HOH   44  644 22  HOH   HOH A . 
G 6 HOH   45  645 9   HOH   HOH A . 
G 6 HOH   46  646 111 HOH   HOH A . 
G 6 HOH   47  647 35  HOH   HOH A . 
G 6 HOH   48  648 55  HOH   HOH A . 
G 6 HOH   49  649 29  HOH   HOH A . 
G 6 HOH   50  650 44  HOH   HOH A . 
G 6 HOH   51  651 75  HOH   HOH A . 
G 6 HOH   52  652 20  HOH   HOH A . 
G 6 HOH   53  653 54  HOH   HOH A . 
G 6 HOH   54  654 25  HOH   HOH A . 
G 6 HOH   55  655 51  HOH   HOH A . 
G 6 HOH   56  656 83  HOH   HOH A . 
G 6 HOH   57  657 19  HOH   HOH A . 
G 6 HOH   58  658 91  HOH   HOH A . 
G 6 HOH   59  659 32  HOH   HOH A . 
G 6 HOH   60  660 43  HOH   HOH A . 
G 6 HOH   61  661 110 HOH   HOH A . 
G 6 HOH   62  662 42  HOH   HOH A . 
G 6 HOH   63  663 80  HOH   HOH A . 
G 6 HOH   64  664 45  HOH   HOH A . 
G 6 HOH   65  665 12  HOH   HOH A . 
G 6 HOH   66  666 37  HOH   HOH A . 
G 6 HOH   67  667 15  HOH   HOH A . 
G 6 HOH   68  668 46  HOH   HOH A . 
G 6 HOH   69  669 41  HOH   HOH A . 
G 6 HOH   70  670 88  HOH   HOH A . 
G 6 HOH   71  671 14  HOH   HOH A . 
G 6 HOH   72  672 57  HOH   HOH A . 
G 6 HOH   73  673 112 HOH   HOH A . 
G 6 HOH   74  674 49  HOH   HOH A . 
G 6 HOH   75  675 79  HOH   HOH A . 
G 6 HOH   76  676 72  HOH   HOH A . 
G 6 HOH   77  677 66  HOH   HOH A . 
G 6 HOH   78  678 64  HOH   HOH A . 
G 6 HOH   79  679 65  HOH   HOH A . 
G 6 HOH   80  680 81  HOH   HOH A . 
G 6 HOH   81  681 94  HOH   HOH A . 
G 6 HOH   82  682 97  HOH   HOH A . 
G 6 HOH   83  683 63  HOH   HOH A . 
G 6 HOH   84  684 82  HOH   HOH A . 
G 6 HOH   85  685 101 HOH   HOH A . 
G 6 HOH   86  686 58  HOH   HOH A . 
G 6 HOH   87  687 103 HOH   HOH A . 
G 6 HOH   88  688 105 HOH   HOH A . 
G 6 HOH   89  689 59  HOH   HOH A . 
G 6 HOH   90  690 90  HOH   HOH A . 
G 6 HOH   91  691 60  HOH   HOH A . 
G 6 HOH   92  692 70  HOH   HOH A . 
G 6 HOH   93  693 78  HOH   HOH A . 
G 6 HOH   94  694 99  HOH   HOH A . 
G 6 HOH   95  695 109 HOH   HOH A . 
G 6 HOH   96  696 56  HOH   HOH A . 
G 6 HOH   97  697 86  HOH   HOH A . 
G 6 HOH   98  698 76  HOH   HOH A . 
G 6 HOH   99  699 73  HOH   HOH A . 
G 6 HOH   100 700 98  HOH   HOH A . 
G 6 HOH   101 701 89  HOH   HOH A . 
G 6 HOH   102 702 48  HOH   HOH A . 
G 6 HOH   103 703 85  HOH   HOH A . 
G 6 HOH   104 704 61  HOH   HOH A . 
G 6 HOH   105 705 106 HOH   HOH A . 
G 6 HOH   106 706 84  HOH   HOH A . 
G 6 HOH   107 707 50  HOH   HOH A . 
G 6 HOH   108 708 62  HOH   HOH A . 
G 6 HOH   109 709 100 HOH   HOH A . 
G 6 HOH   110 710 95  HOH   HOH A . 
G 6 HOH   111 711 104 HOH   HOH A . 
G 6 HOH   112 712 107 HOH   HOH A . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? REFMAC   ? ? ? 5.8.0405 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .        2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .        3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER   ? ? ? 1.3.3    4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8Z35 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     71.439 
_cell.length_a_esd                 ? 
_cell.length_b                     71.439 
_cell.length_b_esd                 ? 
_cell.length_c                     45.660 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         8Z35 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                76 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 41' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   8Z35 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.30 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          46.43 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
;Protein (30mg/ml in 20mM Tril-HCl (pH 7.5), 50mM NaCl), reservoir solution (30% (w/v) PEG MME 5000, 0.2M ammonium sulfate, 0.1M HEPES (pH 7.0))
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            295 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     'IMAGE PLATE' 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         RIGAKU 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2007-06-24 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.5418 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      'ROTATING ANODE' 
_diffrn_source.target                      ? 
_diffrn_source.type                        'RIGAKU FR-E' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.5418 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   ? 
_diffrn_source.pdbx_synchrotron_site       ? 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8Z35 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.0 
_reflns.d_resolution_low                               50.0 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     15794 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.3 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.0 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          55.1 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   ? 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.036 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.0 
_reflns_shell.d_res_low                                     2.07 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           4.7 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1532 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  ? 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.362 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            -0.31 
_refine.aniso_B[1][2]                            -0.00 
_refine.aniso_B[1][3]                            -0.00 
_refine.aniso_B[2][2]                            -0.31 
_refine.aniso_B[2][3]                            -0.00 
_refine.aniso_B[3][3]                            0.62 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               34.123 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.963 
_refine.correlation_coeff_Fo_to_Fc_free          0.950 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 8Z35 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.00 
_refine.ls_d_res_low                             20.00 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     14049 
_refine.ls_number_reflns_R_free                  1614 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.51 
_refine.ls_percent_reflns_R_free                 10.3 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.18791 
_refine.ls_R_factor_R_free                       0.21582 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.18469 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'BABINET MODEL WITH MASK' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.203 
_refine.pdbx_overall_ESU_R_Free                  0.163 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             7.661 
_refine.overall_SU_ML                            0.108 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         1 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.00 
_refine_hist.d_res_low                        20.00 
_refine_hist.number_atoms_solvent             112 
_refine_hist.number_atoms_total               1855 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        1703 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         40 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.002  0.012  1786 ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 0.850  1.660  2411 ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 6.437  5.000  212  ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 3.683  5.000  15   ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 12.222 10.000 293  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.071  0.200  247  ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.003  0.020  1367 ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_gen_planes_other           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbd_refined                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbd_other                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbtor_refined              ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbtor_other                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_xyhbond_nbd_refined        ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_xyhbond_nbd_other          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_metal_ion_refined          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_metal_ion_other            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_vdw_refined       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_vdw_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_hbond_refined     ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_hbond_other       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_metal_ion_refined ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_metal_ion_other   ? ? 
'X-RAY DIFFRACTION' ? 1.097  3.152  854  ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 1.879  5.647  1064 ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 1.428  3.397  932  ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 5.665  37.79  2785 ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_long_range_B_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_rigid_bond_restr           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_sphericity_free            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_sphericity_bonded          ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       2.000 
_refine_ls_shell.d_res_low                        2.051 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             122 
_refine_ls_shell.number_reflns_R_work             993 
_refine_ls_shell.percent_reflns_obs               99.20 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.217 
_refine_ls_shell.redundancy_reflns_all            ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.wR_factor_all                    ? 
_refine_ls_shell.wR_factor_obs                    ? 
_refine_ls_shell.wR_factor_R_free                 ? 
_refine_ls_shell.wR_factor_R_work                 ? 
_refine_ls_shell.pdbx_R_complete                  ? 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.pdbx_phase_error                 ? 
_refine_ls_shell.pdbx_fsc_work                    ? 
_refine_ls_shell.pdbx_fsc_free                    ? 
_refine_ls_shell.R_factor_R_free                  0.291 
# 
_struct.entry_id                     8Z35 
_struct.title                        'Crystal Structure of HIF-PHD2 in complex with compound 7 (DS44470011)' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        8Z35 
_struct_keywords.text            'Renal anemia, Inhibitor, OXIDOREDUCTASE' 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 3 ? 
E N N 4 ? 
F N N 5 ? 
G N N 6 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    EGLN1_HUMAN 
_struct_ref.pdbx_db_accession          Q9GZT9 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;LPALKLALEYIVPCMNKHGICVVDDFLGKETGQQIGDEVRALHDTGKFTDGQLVSQKSDSSKDIRGDKITWIEGKEPGCE
TIGLLMSSMDDLIRHCNGKLGSYKINGRTKAMVACYPGNGTGYVRHVDNPNGDGRCVTCIYYLNKDWDAKVSGGILRIFP
EGKAQFADIEPKFDRLLFFWSDRRNPHEVQPAYATRYAITVWYFDADERARAKVKY
;
_struct_ref.pdbx_align_begin           188 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              8Z35 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 9 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 224 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             Q9GZT9 
_struct_ref_seq.db_align_beg                  188 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  403 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       188 
_struct_ref_seq.pdbx_auth_seq_align_end       403 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 8Z35 MET A 1 ? UNP Q9GZT9 ? ? 'initiating methionine' 180 1 
1 8Z35 ALA A 2 ? UNP Q9GZT9 ? ? 'expression tag'        181 2 
1 8Z35 HIS A 3 ? UNP Q9GZT9 ? ? 'expression tag'        182 3 
1 8Z35 HIS A 4 ? UNP Q9GZT9 ? ? 'expression tag'        183 4 
1 8Z35 HIS A 5 ? UNP Q9GZT9 ? ? 'expression tag'        184 5 
1 8Z35 HIS A 6 ? UNP Q9GZT9 ? ? 'expression tag'        185 6 
1 8Z35 HIS A 7 ? UNP Q9GZT9 ? ? 'expression tag'        186 7 
1 8Z35 HIS A 8 ? UNP Q9GZT9 ? ? 'expression tag'        187 8 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 140   ? 
1 MORE         -14   ? 
1 'SSA (A^2)'  10880 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 PRO A 10  ? TYR A 18  ? PRO A 189 TYR A 197 1 ? 9  
HELX_P HELX_P2 AA2 TYR A 18  ? GLY A 27  ? TYR A 197 GLY A 206 1 ? 10 
HELX_P HELX_P3 AA3 GLY A 36  ? THR A 53  ? GLY A 215 THR A 232 1 ? 18 
HELX_P HELX_P4 AA4 GLY A 59  ? SER A 63  ? GLY A 238 SER A 242 1 ? 5  
HELX_P HELX_P5 AA5 CYS A 87  ? ASN A 105 ? CYS A 266 ASN A 284 1 ? 19 
HELX_P HELX_P6 AA6 ASP A 156 ? GLY A 161 ? ASP A 335 GLY A 340 1 ? 6  
HELX_P HELX_P7 AA7 ALA A 214 ? LYS A 223 ? ALA A 393 LYS A 402 1 ? 10 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? A HIS 134 NE2 ? ? ? 1_555 B FE2   . FE ? ? A HIS 313 A FE2   501 1_555 ? ? ? ? ? ? ? 2.170 ? ? 
metalc2 metalc ? ? A ASP 136 OD1 ? ? ? 1_555 B FE2   . FE ? ? A ASP 315 A FE2   501 1_555 ? ? ? ? ? ? ? 2.300 ? ? 
metalc3 metalc ? ? A HIS 195 NE2 ? ? ? 1_555 B FE2   . FE ? ? A HIS 374 A FE2   501 1_555 ? ? ? ? ? ? ? 2.254 ? ? 
metalc4 metalc ? ? B FE2 .   FE  ? ? ? 1_555 F A1L0X . O2 ? ? A FE2 501 A A1L0X 505 1_555 ? ? ? ? ? ? ? 1.970 ? ? 
metalc5 metalc ? ? B FE2 .   FE  ? ? ? 1_555 F A1L0X . N2 ? ? A FE2 501 A A1L0X 505 1_555 ? ? ? ? ? ? ? 2.029 ? ? 
metalc6 metalc ? ? B FE2 .   FE  ? ? ? 1_555 G HOH   . O  ? ? A FE2 501 A HOH   634 1_555 ? ? ? ? ? ? ? 2.295 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  NE2 ? A HIS   134 ? A HIS   313 ? 1_555 FE ? B FE2 . ? A FE2 501 ? 1_555 OD1 ? A ASP   136 ? A ASP   315 ? 1_555 96.7  ? 
2  NE2 ? A HIS   134 ? A HIS   313 ? 1_555 FE ? B FE2 . ? A FE2 501 ? 1_555 NE2 ? A HIS   195 ? A HIS   374 ? 1_555 87.0  ? 
3  OD1 ? A ASP   136 ? A ASP   315 ? 1_555 FE ? B FE2 . ? A FE2 501 ? 1_555 NE2 ? A HIS   195 ? A HIS   374 ? 1_555 84.7  ? 
4  NE2 ? A HIS   134 ? A HIS   313 ? 1_555 FE ? B FE2 . ? A FE2 501 ? 1_555 O2  ? F A1L0X .   ? A A1L0X 505 ? 1_555 99.2  ? 
5  OD1 ? A ASP   136 ? A ASP   315 ? 1_555 FE ? B FE2 . ? A FE2 501 ? 1_555 O2  ? F A1L0X .   ? A A1L0X 505 ? 1_555 159.5 ? 
6  NE2 ? A HIS   195 ? A HIS   374 ? 1_555 FE ? B FE2 . ? A FE2 501 ? 1_555 O2  ? F A1L0X .   ? A A1L0X 505 ? 1_555 83.3  ? 
7  NE2 ? A HIS   134 ? A HIS   313 ? 1_555 FE ? B FE2 . ? A FE2 501 ? 1_555 N2  ? F A1L0X .   ? A A1L0X 505 ? 1_555 80.8  ? 
8  OD1 ? A ASP   136 ? A ASP   315 ? 1_555 FE ? B FE2 . ? A FE2 501 ? 1_555 N2  ? F A1L0X .   ? A A1L0X 505 ? 1_555 111.0 ? 
9  NE2 ? A HIS   195 ? A HIS   374 ? 1_555 FE ? B FE2 . ? A FE2 501 ? 1_555 N2  ? F A1L0X .   ? A A1L0X 505 ? 1_555 161.0 ? 
10 O2  ? F A1L0X .   ? A A1L0X 505 ? 1_555 FE ? B FE2 . ? A FE2 501 ? 1_555 N2  ? F A1L0X .   ? A A1L0X 505 ? 1_555 84.4  ? 
11 NE2 ? A HIS   134 ? A HIS   313 ? 1_555 FE ? B FE2 . ? A FE2 501 ? 1_555 O   ? G HOH   .   ? A HOH   634 ? 1_555 179.4 ? 
12 OD1 ? A ASP   136 ? A ASP   315 ? 1_555 FE ? B FE2 . ? A FE2 501 ? 1_555 O   ? G HOH   .   ? A HOH   634 ? 1_555 83.1  ? 
13 NE2 ? A HIS   195 ? A HIS   374 ? 1_555 FE ? B FE2 . ? A FE2 501 ? 1_555 O   ? G HOH   .   ? A HOH   634 ? 1_555 92.4  ? 
14 O2  ? F A1L0X .   ? A A1L0X 505 ? 1_555 FE ? B FE2 . ? A FE2 501 ? 1_555 O   ? G HOH   .   ? A HOH   634 ? 1_555 80.9  ? 
15 N2  ? F A1L0X .   ? A A1L0X 505 ? 1_555 FE ? B FE2 . ? A FE2 501 ? 1_555 O   ? G HOH   .   ? A HOH   634 ? 1_555 99.8  ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 7 ? 
AA2 ? 5 ? 
AA3 ? 4 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 ILE A 28  ? VAL A 31  ? ILE A 207 VAL A 210 
AA1 2 ARG A 183 ? TRP A 188 ? ARG A 362 TRP A 367 
AA1 3 ARG A 143 ? TYR A 150 ? ARG A 322 TYR A 329 
AA1 4 THR A 203 ? ASP A 213 ? THR A 382 ASP A 392 
AA1 5 ALA A 119 ? PRO A 125 ? ALA A 298 PRO A 304 
AA1 6 LYS A 76  ? ILE A 80  ? LYS A 255 ILE A 259 
AA1 7 THR A 57  ? ASP A 58  ? THR A 236 ASP A 237 
AA2 1 ILE A 28  ? VAL A 31  ? ILE A 207 VAL A 210 
AA2 2 ARG A 183 ? TRP A 188 ? ARG A 362 TRP A 367 
AA2 3 ARG A 143 ? TYR A 150 ? ARG A 322 TYR A 329 
AA2 4 THR A 203 ? ASP A 213 ? THR A 382 ASP A 392 
AA2 5 ILE A 113 ? ARG A 116 ? ILE A 292 ARG A 295 
AA3 1 THR A 129 ? HIS A 134 ? THR A 308 HIS A 313 
AA3 2 HIS A 195 ? ALA A 200 ? HIS A 374 ALA A 379 
AA3 3 LEU A 164 ? ILE A 166 ? LEU A 343 ILE A 345 
AA3 4 ALA A 175 ? ILE A 177 ? ALA A 354 ILE A 356 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N VAL A 31  ? N VAL A 210 O LEU A 184 ? O LEU A 363 
AA1 2 3 O PHE A 187 ? O PHE A 366 N THR A 146 ? N THR A 325 
AA1 3 4 N TYR A 149 ? N TYR A 328 O ILE A 207 ? O ILE A 386 
AA1 4 5 O THR A 208 ? O THR A 387 N MET A 120 ? N MET A 299 
AA1 5 6 O VAL A 121 ? O VAL A 300 N THR A 78  ? N THR A 257 
AA1 6 7 O ILE A 77  ? O ILE A 256 N THR A 57  ? N THR A 236 
AA2 1 2 N VAL A 31  ? N VAL A 210 O LEU A 184 ? O LEU A 363 
AA2 2 3 O PHE A 187 ? O PHE A 366 N THR A 146 ? N THR A 325 
AA2 3 4 N TYR A 149 ? N TYR A 328 O ILE A 207 ? O ILE A 386 
AA2 4 5 O PHE A 212 ? O PHE A 391 N GLY A 115 ? N GLY A 294 
AA3 1 2 N THR A 129 ? N THR A 308 O ALA A 200 ? O ALA A 379 
AA3 2 3 O GLU A 196 ? O GLU A 375 N ARG A 165 ? N ARG A 344 
AA3 3 4 N LEU A 164 ? N LEU A 343 O ILE A 177 ? O ILE A 356 
# 
_pdbx_entry_details.entry_id                   8Z35 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 TYR A 197 ? ? -138.92 -61.05 
2 1 PRO A 304 ? ? -75.77  27.86  
3 1 LEU A 330 ? ? -141.59 37.43  
# 
_pdbx_refine_tls.id               1 
_pdbx_refine_tls.pdbx_refine_id   'X-RAY DIFFRACTION' 
_pdbx_refine_tls.details          ? 
_pdbx_refine_tls.method           refined 
_pdbx_refine_tls.origin_x         23.9415 
_pdbx_refine_tls.origin_y         -8.2278 
_pdbx_refine_tls.origin_z         2.4534 
_pdbx_refine_tls.T[1][1]          0.0042 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          0.0042 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          0.0052 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          0.0615 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          0.0081 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          0.0087 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          1.5046 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          0.5117 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          0.0660 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          1.0385 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          0.2120 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          1.4298 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          -0.0029 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          -0.0100 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          -0.0010 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          0.0125 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          -0.0507 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          -0.0237 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          0.0329 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          -0.1162 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          0.0536 
_pdbx_refine_tls.S[3][3]_esd      ? 
# 
_pdbx_refine_tls_group.id                  1 
_pdbx_refine_tls_group.pdbx_refine_id      'X-RAY DIFFRACTION' 
_pdbx_refine_tls_group.refine_tls_id       1 
_pdbx_refine_tls_group.beg_label_asym_id   ? 
_pdbx_refine_tls_group.beg_label_seq_id    ? 
_pdbx_refine_tls_group.beg_auth_asym_id    A 
_pdbx_refine_tls_group.beg_auth_seq_id     182 
_pdbx_refine_tls_group.beg_PDB_ins_code    ? 
_pdbx_refine_tls_group.end_label_asym_id   ? 
_pdbx_refine_tls_group.end_label_seq_id    ? 
_pdbx_refine_tls_group.end_auth_asym_id    A 
_pdbx_refine_tls_group.end_auth_seq_id     402 
_pdbx_refine_tls_group.end_PDB_ins_code    ? 
_pdbx_refine_tls_group.selection           ? 
_pdbx_refine_tls_group.selection_details   ? 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A MET 180 ? A MET 1   
2  1 Y 1 A ALA 181 ? A ALA 2   
3  1 Y 1 A GLN 243 ? A GLN 64  
4  1 Y 1 A LYS 244 ? A LYS 65  
5  1 Y 1 A SER 245 ? A SER 66  
6  1 Y 1 A ASP 246 ? A ASP 67  
7  1 Y 1 A SER 247 ? A SER 68  
8  1 Y 1 A SER 248 ? A SER 69  
9  1 Y 1 A LYS 249 ? A LYS 70  
10 1 Y 1 A TYR 403 ? A TYR 224 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
A1L0X C1   C  Y N 1   
A1L0X C2   C  Y N 2   
A1L0X C3   C  Y N 3   
A1L0X C7   C  N N 4   
A1L0X C6   C  N N 5   
A1L0X O2   O  N N 6   
A1L0X C4   C  Y N 7   
A1L0X C5   C  N N 8   
A1L0X O3   O  N N 9   
A1L0X C11  C  Y N 10  
A1L0X C13  C  Y N 11  
A1L0X C15  C  Y N 12  
A1L0X N1   N  Y N 13  
A1L0X C18  C  Y N 14  
A1L0X C10  C  Y N 15  
A1L0X C12  C  Y N 16  
A1L0X C14  C  Y N 17  
A1L0X C16  C  Y N 18  
A1L0X C17  C  Y N 19  
A1L0X C19  C  Y N 20  
A1L0X O1   O  N N 21  
A1L0X N2   N  Y N 22  
A1L0X C8   C  N N 23  
A1L0X C9   C  N N 24  
A1L0X O4   O  N N 25  
A1L0X N3   N  N N 26  
A1L0X C20  C  Y N 27  
A1L0X C21  C  Y N 28  
A1L0X H1   H  N N 29  
A1L0X H2   H  N N 30  
A1L0X H3   H  N N 31  
A1L0X H4   H  N N 32  
A1L0X H5   H  N N 33  
A1L0X H6   H  N N 34  
A1L0X H7   H  N N 35  
A1L0X H8   H  N N 36  
A1L0X H9   H  N N 37  
A1L0X H10  H  N N 38  
A1L0X H11  H  N N 39  
A1L0X H12  H  N N 40  
A1L0X H13  H  N N 41  
A1L0X H14  H  N N 42  
A1L0X H15  H  N N 43  
A1L0X H16  H  N N 44  
A1L0X H17  H  N N 45  
A1L0X H18  H  N N 46  
A1L0X H19  H  N N 47  
ALA   N    N  N N 48  
ALA   CA   C  N S 49  
ALA   C    C  N N 50  
ALA   O    O  N N 51  
ALA   CB   C  N N 52  
ALA   OXT  O  N N 53  
ALA   H    H  N N 54  
ALA   H2   H  N N 55  
ALA   HA   H  N N 56  
ALA   HB1  H  N N 57  
ALA   HB2  H  N N 58  
ALA   HB3  H  N N 59  
ALA   HXT  H  N N 60  
ARG   N    N  N N 61  
ARG   CA   C  N S 62  
ARG   C    C  N N 63  
ARG   O    O  N N 64  
ARG   CB   C  N N 65  
ARG   CG   C  N N 66  
ARG   CD   C  N N 67  
ARG   NE   N  N N 68  
ARG   CZ   C  N N 69  
ARG   NH1  N  N N 70  
ARG   NH2  N  N N 71  
ARG   OXT  O  N N 72  
ARG   H    H  N N 73  
ARG   H2   H  N N 74  
ARG   HA   H  N N 75  
ARG   HB2  H  N N 76  
ARG   HB3  H  N N 77  
ARG   HG2  H  N N 78  
ARG   HG3  H  N N 79  
ARG   HD2  H  N N 80  
ARG   HD3  H  N N 81  
ARG   HE   H  N N 82  
ARG   HH11 H  N N 83  
ARG   HH12 H  N N 84  
ARG   HH21 H  N N 85  
ARG   HH22 H  N N 86  
ARG   HXT  H  N N 87  
ASN   N    N  N N 88  
ASN   CA   C  N S 89  
ASN   C    C  N N 90  
ASN   O    O  N N 91  
ASN   CB   C  N N 92  
ASN   CG   C  N N 93  
ASN   OD1  O  N N 94  
ASN   ND2  N  N N 95  
ASN   OXT  O  N N 96  
ASN   H    H  N N 97  
ASN   H2   H  N N 98  
ASN   HA   H  N N 99  
ASN   HB2  H  N N 100 
ASN   HB3  H  N N 101 
ASN   HD21 H  N N 102 
ASN   HD22 H  N N 103 
ASN   HXT  H  N N 104 
ASP   N    N  N N 105 
ASP   CA   C  N S 106 
ASP   C    C  N N 107 
ASP   O    O  N N 108 
ASP   CB   C  N N 109 
ASP   CG   C  N N 110 
ASP   OD1  O  N N 111 
ASP   OD2  O  N N 112 
ASP   OXT  O  N N 113 
ASP   H    H  N N 114 
ASP   H2   H  N N 115 
ASP   HA   H  N N 116 
ASP   HB2  H  N N 117 
ASP   HB3  H  N N 118 
ASP   HD2  H  N N 119 
ASP   HXT  H  N N 120 
CL    CL   CL N N 121 
CYS   N    N  N N 122 
CYS   CA   C  N R 123 
CYS   C    C  N N 124 
CYS   O    O  N N 125 
CYS   CB   C  N N 126 
CYS   SG   S  N N 127 
CYS   OXT  O  N N 128 
CYS   H    H  N N 129 
CYS   H2   H  N N 130 
CYS   HA   H  N N 131 
CYS   HB2  H  N N 132 
CYS   HB3  H  N N 133 
CYS   HG   H  N N 134 
CYS   HXT  H  N N 135 
FE2   FE   FE N N 136 
GLN   N    N  N N 137 
GLN   CA   C  N S 138 
GLN   C    C  N N 139 
GLN   O    O  N N 140 
GLN   CB   C  N N 141 
GLN   CG   C  N N 142 
GLN   CD   C  N N 143 
GLN   OE1  O  N N 144 
GLN   NE2  N  N N 145 
GLN   OXT  O  N N 146 
GLN   H    H  N N 147 
GLN   H2   H  N N 148 
GLN   HA   H  N N 149 
GLN   HB2  H  N N 150 
GLN   HB3  H  N N 151 
GLN   HG2  H  N N 152 
GLN   HG3  H  N N 153 
GLN   HE21 H  N N 154 
GLN   HE22 H  N N 155 
GLN   HXT  H  N N 156 
GLU   N    N  N N 157 
GLU   CA   C  N S 158 
GLU   C    C  N N 159 
GLU   O    O  N N 160 
GLU   CB   C  N N 161 
GLU   CG   C  N N 162 
GLU   CD   C  N N 163 
GLU   OE1  O  N N 164 
GLU   OE2  O  N N 165 
GLU   OXT  O  N N 166 
GLU   H    H  N N 167 
GLU   H2   H  N N 168 
GLU   HA   H  N N 169 
GLU   HB2  H  N N 170 
GLU   HB3  H  N N 171 
GLU   HG2  H  N N 172 
GLU   HG3  H  N N 173 
GLU   HE2  H  N N 174 
GLU   HXT  H  N N 175 
GLY   N    N  N N 176 
GLY   CA   C  N N 177 
GLY   C    C  N N 178 
GLY   O    O  N N 179 
GLY   OXT  O  N N 180 
GLY   H    H  N N 181 
GLY   H2   H  N N 182 
GLY   HA2  H  N N 183 
GLY   HA3  H  N N 184 
GLY   HXT  H  N N 185 
HIS   N    N  N N 186 
HIS   CA   C  N S 187 
HIS   C    C  N N 188 
HIS   O    O  N N 189 
HIS   CB   C  N N 190 
HIS   CG   C  Y N 191 
HIS   ND1  N  Y N 192 
HIS   CD2  C  Y N 193 
HIS   CE1  C  Y N 194 
HIS   NE2  N  Y N 195 
HIS   OXT  O  N N 196 
HIS   H    H  N N 197 
HIS   H2   H  N N 198 
HIS   HA   H  N N 199 
HIS   HB2  H  N N 200 
HIS   HB3  H  N N 201 
HIS   HD1  H  N N 202 
HIS   HD2  H  N N 203 
HIS   HE1  H  N N 204 
HIS   HE2  H  N N 205 
HIS   HXT  H  N N 206 
HOH   O    O  N N 207 
HOH   H1   H  N N 208 
HOH   H2   H  N N 209 
ILE   N    N  N N 210 
ILE   CA   C  N S 211 
ILE   C    C  N N 212 
ILE   O    O  N N 213 
ILE   CB   C  N S 214 
ILE   CG1  C  N N 215 
ILE   CG2  C  N N 216 
ILE   CD1  C  N N 217 
ILE   OXT  O  N N 218 
ILE   H    H  N N 219 
ILE   H2   H  N N 220 
ILE   HA   H  N N 221 
ILE   HB   H  N N 222 
ILE   HG12 H  N N 223 
ILE   HG13 H  N N 224 
ILE   HG21 H  N N 225 
ILE   HG22 H  N N 226 
ILE   HG23 H  N N 227 
ILE   HD11 H  N N 228 
ILE   HD12 H  N N 229 
ILE   HD13 H  N N 230 
ILE   HXT  H  N N 231 
LEU   N    N  N N 232 
LEU   CA   C  N S 233 
LEU   C    C  N N 234 
LEU   O    O  N N 235 
LEU   CB   C  N N 236 
LEU   CG   C  N N 237 
LEU   CD1  C  N N 238 
LEU   CD2  C  N N 239 
LEU   OXT  O  N N 240 
LEU   H    H  N N 241 
LEU   H2   H  N N 242 
LEU   HA   H  N N 243 
LEU   HB2  H  N N 244 
LEU   HB3  H  N N 245 
LEU   HG   H  N N 246 
LEU   HD11 H  N N 247 
LEU   HD12 H  N N 248 
LEU   HD13 H  N N 249 
LEU   HD21 H  N N 250 
LEU   HD22 H  N N 251 
LEU   HD23 H  N N 252 
LEU   HXT  H  N N 253 
LYS   N    N  N N 254 
LYS   CA   C  N S 255 
LYS   C    C  N N 256 
LYS   O    O  N N 257 
LYS   CB   C  N N 258 
LYS   CG   C  N N 259 
LYS   CD   C  N N 260 
LYS   CE   C  N N 261 
LYS   NZ   N  N N 262 
LYS   OXT  O  N N 263 
LYS   H    H  N N 264 
LYS   H2   H  N N 265 
LYS   HA   H  N N 266 
LYS   HB2  H  N N 267 
LYS   HB3  H  N N 268 
LYS   HG2  H  N N 269 
LYS   HG3  H  N N 270 
LYS   HD2  H  N N 271 
LYS   HD3  H  N N 272 
LYS   HE2  H  N N 273 
LYS   HE3  H  N N 274 
LYS   HZ1  H  N N 275 
LYS   HZ2  H  N N 276 
LYS   HZ3  H  N N 277 
LYS   HXT  H  N N 278 
MET   N    N  N N 279 
MET   CA   C  N S 280 
MET   C    C  N N 281 
MET   O    O  N N 282 
MET   CB   C  N N 283 
MET   CG   C  N N 284 
MET   SD   S  N N 285 
MET   CE   C  N N 286 
MET   OXT  O  N N 287 
MET   H    H  N N 288 
MET   H2   H  N N 289 
MET   HA   H  N N 290 
MET   HB2  H  N N 291 
MET   HB3  H  N N 292 
MET   HG2  H  N N 293 
MET   HG3  H  N N 294 
MET   HE1  H  N N 295 
MET   HE2  H  N N 296 
MET   HE3  H  N N 297 
MET   HXT  H  N N 298 
PHE   N    N  N N 299 
PHE   CA   C  N S 300 
PHE   C    C  N N 301 
PHE   O    O  N N 302 
PHE   CB   C  N N 303 
PHE   CG   C  Y N 304 
PHE   CD1  C  Y N 305 
PHE   CD2  C  Y N 306 
PHE   CE1  C  Y N 307 
PHE   CE2  C  Y N 308 
PHE   CZ   C  Y N 309 
PHE   OXT  O  N N 310 
PHE   H    H  N N 311 
PHE   H2   H  N N 312 
PHE   HA   H  N N 313 
PHE   HB2  H  N N 314 
PHE   HB3  H  N N 315 
PHE   HD1  H  N N 316 
PHE   HD2  H  N N 317 
PHE   HE1  H  N N 318 
PHE   HE2  H  N N 319 
PHE   HZ   H  N N 320 
PHE   HXT  H  N N 321 
PRO   N    N  N N 322 
PRO   CA   C  N S 323 
PRO   C    C  N N 324 
PRO   O    O  N N 325 
PRO   CB   C  N N 326 
PRO   CG   C  N N 327 
PRO   CD   C  N N 328 
PRO   OXT  O  N N 329 
PRO   H    H  N N 330 
PRO   HA   H  N N 331 
PRO   HB2  H  N N 332 
PRO   HB3  H  N N 333 
PRO   HG2  H  N N 334 
PRO   HG3  H  N N 335 
PRO   HD2  H  N N 336 
PRO   HD3  H  N N 337 
PRO   HXT  H  N N 338 
SER   N    N  N N 339 
SER   CA   C  N S 340 
SER   C    C  N N 341 
SER   O    O  N N 342 
SER   CB   C  N N 343 
SER   OG   O  N N 344 
SER   OXT  O  N N 345 
SER   H    H  N N 346 
SER   H2   H  N N 347 
SER   HA   H  N N 348 
SER   HB2  H  N N 349 
SER   HB3  H  N N 350 
SER   HG   H  N N 351 
SER   HXT  H  N N 352 
SO4   S    S  N N 353 
SO4   O1   O  N N 354 
SO4   O2   O  N N 355 
SO4   O3   O  N N 356 
SO4   O4   O  N N 357 
THR   N    N  N N 358 
THR   CA   C  N S 359 
THR   C    C  N N 360 
THR   O    O  N N 361 
THR   CB   C  N R 362 
THR   OG1  O  N N 363 
THR   CG2  C  N N 364 
THR   OXT  O  N N 365 
THR   H    H  N N 366 
THR   H2   H  N N 367 
THR   HA   H  N N 368 
THR   HB   H  N N 369 
THR   HG1  H  N N 370 
THR   HG21 H  N N 371 
THR   HG22 H  N N 372 
THR   HG23 H  N N 373 
THR   HXT  H  N N 374 
TRP   N    N  N N 375 
TRP   CA   C  N S 376 
TRP   C    C  N N 377 
TRP   O    O  N N 378 
TRP   CB   C  N N 379 
TRP   CG   C  Y N 380 
TRP   CD1  C  Y N 381 
TRP   CD2  C  Y N 382 
TRP   NE1  N  Y N 383 
TRP   CE2  C  Y N 384 
TRP   CE3  C  Y N 385 
TRP   CZ2  C  Y N 386 
TRP   CZ3  C  Y N 387 
TRP   CH2  C  Y N 388 
TRP   OXT  O  N N 389 
TRP   H    H  N N 390 
TRP   H2   H  N N 391 
TRP   HA   H  N N 392 
TRP   HB2  H  N N 393 
TRP   HB3  H  N N 394 
TRP   HD1  H  N N 395 
TRP   HE1  H  N N 396 
TRP   HE3  H  N N 397 
TRP   HZ2  H  N N 398 
TRP   HZ3  H  N N 399 
TRP   HH2  H  N N 400 
TRP   HXT  H  N N 401 
TYR   N    N  N N 402 
TYR   CA   C  N S 403 
TYR   C    C  N N 404 
TYR   O    O  N N 405 
TYR   CB   C  N N 406 
TYR   CG   C  Y N 407 
TYR   CD1  C  Y N 408 
TYR   CD2  C  Y N 409 
TYR   CE1  C  Y N 410 
TYR   CE2  C  Y N 411 
TYR   CZ   C  Y N 412 
TYR   OH   O  N N 413 
TYR   OXT  O  N N 414 
TYR   H    H  N N 415 
TYR   H2   H  N N 416 
TYR   HA   H  N N 417 
TYR   HB2  H  N N 418 
TYR   HB3  H  N N 419 
TYR   HD1  H  N N 420 
TYR   HD2  H  N N 421 
TYR   HE1  H  N N 422 
TYR   HE2  H  N N 423 
TYR   HH   H  N N 424 
TYR   HXT  H  N N 425 
VAL   N    N  N N 426 
VAL   CA   C  N S 427 
VAL   C    C  N N 428 
VAL   O    O  N N 429 
VAL   CB   C  N N 430 
VAL   CG1  C  N N 431 
VAL   CG2  C  N N 432 
VAL   OXT  O  N N 433 
VAL   H    H  N N 434 
VAL   H2   H  N N 435 
VAL   HA   H  N N 436 
VAL   HB   H  N N 437 
VAL   HG11 H  N N 438 
VAL   HG12 H  N N 439 
VAL   HG13 H  N N 440 
VAL   HG21 H  N N 441 
VAL   HG22 H  N N 442 
VAL   HG23 H  N N 443 
VAL   HXT  H  N N 444 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
A1L0X C18 C17  doub Y N 1   
A1L0X C18 C19  sing Y N 2   
A1L0X C17 C16  sing Y N 3   
A1L0X C14 C15  doub Y N 4   
A1L0X C14 C13  sing Y N 5   
A1L0X C15 C10  sing Y N 6   
A1L0X C19 C20  doub Y N 7   
A1L0X C16 C13  sing N N 8   
A1L0X C16 C21  doub Y N 9   
A1L0X C13 C12  doub Y N 10  
A1L0X C10 C5   sing N N 11  
A1L0X C10 C11  doub Y N 12  
A1L0X C5  C2   sing N N 13  
A1L0X C20 C21  sing Y N 14  
A1L0X C12 C11  sing Y N 15  
A1L0X C2  N2   doub Y N 16  
A1L0X C2  N1   sing Y N 17  
A1L0X N2  C3   sing Y N 18  
A1L0X N1  C1   doub Y N 19  
A1L0X O2  C6   doub N N 20  
A1L0X C1  C9   sing N N 21  
A1L0X C1  C4   sing Y N 22  
A1L0X C3  C6   sing N N 23  
A1L0X C3  C4   doub Y N 24  
A1L0X C6  N3   sing N N 25  
A1L0X C4  O1   sing N N 26  
A1L0X N3  C7   sing N N 27  
A1L0X C7  C8   sing N N 28  
A1L0X C8  O4   doub N N 29  
A1L0X C8  O3   sing N N 30  
A1L0X C7  H1   sing N N 31  
A1L0X C5  H2   sing N N 32  
A1L0X C5  H3   sing N N 33  
A1L0X O3  H4   sing N N 34  
A1L0X C11 H5   sing N N 35  
A1L0X C15 H6   sing N N 36  
A1L0X C18 H7   sing N N 37  
A1L0X C12 H8   sing N N 38  
A1L0X C14 H9   sing N N 39  
A1L0X C17 H10  sing N N 40  
A1L0X C19 H11  sing N N 41  
A1L0X O1  H12  sing N N 42  
A1L0X C9  H13  sing N N 43  
A1L0X C9  H14  sing N N 44  
A1L0X C9  H15  sing N N 45  
A1L0X C20 H16  sing N N 46  
A1L0X C21 H17  sing N N 47  
A1L0X C7  H18  sing N N 48  
A1L0X N3  H19  sing N N 49  
ALA   N   CA   sing N N 50  
ALA   N   H    sing N N 51  
ALA   N   H2   sing N N 52  
ALA   CA  C    sing N N 53  
ALA   CA  CB   sing N N 54  
ALA   CA  HA   sing N N 55  
ALA   C   O    doub N N 56  
ALA   C   OXT  sing N N 57  
ALA   CB  HB1  sing N N 58  
ALA   CB  HB2  sing N N 59  
ALA   CB  HB3  sing N N 60  
ALA   OXT HXT  sing N N 61  
ARG   N   CA   sing N N 62  
ARG   N   H    sing N N 63  
ARG   N   H2   sing N N 64  
ARG   CA  C    sing N N 65  
ARG   CA  CB   sing N N 66  
ARG   CA  HA   sing N N 67  
ARG   C   O    doub N N 68  
ARG   C   OXT  sing N N 69  
ARG   CB  CG   sing N N 70  
ARG   CB  HB2  sing N N 71  
ARG   CB  HB3  sing N N 72  
ARG   CG  CD   sing N N 73  
ARG   CG  HG2  sing N N 74  
ARG   CG  HG3  sing N N 75  
ARG   CD  NE   sing N N 76  
ARG   CD  HD2  sing N N 77  
ARG   CD  HD3  sing N N 78  
ARG   NE  CZ   sing N N 79  
ARG   NE  HE   sing N N 80  
ARG   CZ  NH1  sing N N 81  
ARG   CZ  NH2  doub N N 82  
ARG   NH1 HH11 sing N N 83  
ARG   NH1 HH12 sing N N 84  
ARG   NH2 HH21 sing N N 85  
ARG   NH2 HH22 sing N N 86  
ARG   OXT HXT  sing N N 87  
ASN   N   CA   sing N N 88  
ASN   N   H    sing N N 89  
ASN   N   H2   sing N N 90  
ASN   CA  C    sing N N 91  
ASN   CA  CB   sing N N 92  
ASN   CA  HA   sing N N 93  
ASN   C   O    doub N N 94  
ASN   C   OXT  sing N N 95  
ASN   CB  CG   sing N N 96  
ASN   CB  HB2  sing N N 97  
ASN   CB  HB3  sing N N 98  
ASN   CG  OD1  doub N N 99  
ASN   CG  ND2  sing N N 100 
ASN   ND2 HD21 sing N N 101 
ASN   ND2 HD22 sing N N 102 
ASN   OXT HXT  sing N N 103 
ASP   N   CA   sing N N 104 
ASP   N   H    sing N N 105 
ASP   N   H2   sing N N 106 
ASP   CA  C    sing N N 107 
ASP   CA  CB   sing N N 108 
ASP   CA  HA   sing N N 109 
ASP   C   O    doub N N 110 
ASP   C   OXT  sing N N 111 
ASP   CB  CG   sing N N 112 
ASP   CB  HB2  sing N N 113 
ASP   CB  HB3  sing N N 114 
ASP   CG  OD1  doub N N 115 
ASP   CG  OD2  sing N N 116 
ASP   OD2 HD2  sing N N 117 
ASP   OXT HXT  sing N N 118 
CYS   N   CA   sing N N 119 
CYS   N   H    sing N N 120 
CYS   N   H2   sing N N 121 
CYS   CA  C    sing N N 122 
CYS   CA  CB   sing N N 123 
CYS   CA  HA   sing N N 124 
CYS   C   O    doub N N 125 
CYS   C   OXT  sing N N 126 
CYS   CB  SG   sing N N 127 
CYS   CB  HB2  sing N N 128 
CYS   CB  HB3  sing N N 129 
CYS   SG  HG   sing N N 130 
CYS   OXT HXT  sing N N 131 
GLN   N   CA   sing N N 132 
GLN   N   H    sing N N 133 
GLN   N   H2   sing N N 134 
GLN   CA  C    sing N N 135 
GLN   CA  CB   sing N N 136 
GLN   CA  HA   sing N N 137 
GLN   C   O    doub N N 138 
GLN   C   OXT  sing N N 139 
GLN   CB  CG   sing N N 140 
GLN   CB  HB2  sing N N 141 
GLN   CB  HB3  sing N N 142 
GLN   CG  CD   sing N N 143 
GLN   CG  HG2  sing N N 144 
GLN   CG  HG3  sing N N 145 
GLN   CD  OE1  doub N N 146 
GLN   CD  NE2  sing N N 147 
GLN   NE2 HE21 sing N N 148 
GLN   NE2 HE22 sing N N 149 
GLN   OXT HXT  sing N N 150 
GLU   N   CA   sing N N 151 
GLU   N   H    sing N N 152 
GLU   N   H2   sing N N 153 
GLU   CA  C    sing N N 154 
GLU   CA  CB   sing N N 155 
GLU   CA  HA   sing N N 156 
GLU   C   O    doub N N 157 
GLU   C   OXT  sing N N 158 
GLU   CB  CG   sing N N 159 
GLU   CB  HB2  sing N N 160 
GLU   CB  HB3  sing N N 161 
GLU   CG  CD   sing N N 162 
GLU   CG  HG2  sing N N 163 
GLU   CG  HG3  sing N N 164 
GLU   CD  OE1  doub N N 165 
GLU   CD  OE2  sing N N 166 
GLU   OE2 HE2  sing N N 167 
GLU   OXT HXT  sing N N 168 
GLY   N   CA   sing N N 169 
GLY   N   H    sing N N 170 
GLY   N   H2   sing N N 171 
GLY   CA  C    sing N N 172 
GLY   CA  HA2  sing N N 173 
GLY   CA  HA3  sing N N 174 
GLY   C   O    doub N N 175 
GLY   C   OXT  sing N N 176 
GLY   OXT HXT  sing N N 177 
HIS   N   CA   sing N N 178 
HIS   N   H    sing N N 179 
HIS   N   H2   sing N N 180 
HIS   CA  C    sing N N 181 
HIS   CA  CB   sing N N 182 
HIS   CA  HA   sing N N 183 
HIS   C   O    doub N N 184 
HIS   C   OXT  sing N N 185 
HIS   CB  CG   sing N N 186 
HIS   CB  HB2  sing N N 187 
HIS   CB  HB3  sing N N 188 
HIS   CG  ND1  sing Y N 189 
HIS   CG  CD2  doub Y N 190 
HIS   ND1 CE1  doub Y N 191 
HIS   ND1 HD1  sing N N 192 
HIS   CD2 NE2  sing Y N 193 
HIS   CD2 HD2  sing N N 194 
HIS   CE1 NE2  sing Y N 195 
HIS   CE1 HE1  sing N N 196 
HIS   NE2 HE2  sing N N 197 
HIS   OXT HXT  sing N N 198 
HOH   O   H1   sing N N 199 
HOH   O   H2   sing N N 200 
ILE   N   CA   sing N N 201 
ILE   N   H    sing N N 202 
ILE   N   H2   sing N N 203 
ILE   CA  C    sing N N 204 
ILE   CA  CB   sing N N 205 
ILE   CA  HA   sing N N 206 
ILE   C   O    doub N N 207 
ILE   C   OXT  sing N N 208 
ILE   CB  CG1  sing N N 209 
ILE   CB  CG2  sing N N 210 
ILE   CB  HB   sing N N 211 
ILE   CG1 CD1  sing N N 212 
ILE   CG1 HG12 sing N N 213 
ILE   CG1 HG13 sing N N 214 
ILE   CG2 HG21 sing N N 215 
ILE   CG2 HG22 sing N N 216 
ILE   CG2 HG23 sing N N 217 
ILE   CD1 HD11 sing N N 218 
ILE   CD1 HD12 sing N N 219 
ILE   CD1 HD13 sing N N 220 
ILE   OXT HXT  sing N N 221 
LEU   N   CA   sing N N 222 
LEU   N   H    sing N N 223 
LEU   N   H2   sing N N 224 
LEU   CA  C    sing N N 225 
LEU   CA  CB   sing N N 226 
LEU   CA  HA   sing N N 227 
LEU   C   O    doub N N 228 
LEU   C   OXT  sing N N 229 
LEU   CB  CG   sing N N 230 
LEU   CB  HB2  sing N N 231 
LEU   CB  HB3  sing N N 232 
LEU   CG  CD1  sing N N 233 
LEU   CG  CD2  sing N N 234 
LEU   CG  HG   sing N N 235 
LEU   CD1 HD11 sing N N 236 
LEU   CD1 HD12 sing N N 237 
LEU   CD1 HD13 sing N N 238 
LEU   CD2 HD21 sing N N 239 
LEU   CD2 HD22 sing N N 240 
LEU   CD2 HD23 sing N N 241 
LEU   OXT HXT  sing N N 242 
LYS   N   CA   sing N N 243 
LYS   N   H    sing N N 244 
LYS   N   H2   sing N N 245 
LYS   CA  C    sing N N 246 
LYS   CA  CB   sing N N 247 
LYS   CA  HA   sing N N 248 
LYS   C   O    doub N N 249 
LYS   C   OXT  sing N N 250 
LYS   CB  CG   sing N N 251 
LYS   CB  HB2  sing N N 252 
LYS   CB  HB3  sing N N 253 
LYS   CG  CD   sing N N 254 
LYS   CG  HG2  sing N N 255 
LYS   CG  HG3  sing N N 256 
LYS   CD  CE   sing N N 257 
LYS   CD  HD2  sing N N 258 
LYS   CD  HD3  sing N N 259 
LYS   CE  NZ   sing N N 260 
LYS   CE  HE2  sing N N 261 
LYS   CE  HE3  sing N N 262 
LYS   NZ  HZ1  sing N N 263 
LYS   NZ  HZ2  sing N N 264 
LYS   NZ  HZ3  sing N N 265 
LYS   OXT HXT  sing N N 266 
MET   N   CA   sing N N 267 
MET   N   H    sing N N 268 
MET   N   H2   sing N N 269 
MET   CA  C    sing N N 270 
MET   CA  CB   sing N N 271 
MET   CA  HA   sing N N 272 
MET   C   O    doub N N 273 
MET   C   OXT  sing N N 274 
MET   CB  CG   sing N N 275 
MET   CB  HB2  sing N N 276 
MET   CB  HB3  sing N N 277 
MET   CG  SD   sing N N 278 
MET   CG  HG2  sing N N 279 
MET   CG  HG3  sing N N 280 
MET   SD  CE   sing N N 281 
MET   CE  HE1  sing N N 282 
MET   CE  HE2  sing N N 283 
MET   CE  HE3  sing N N 284 
MET   OXT HXT  sing N N 285 
PHE   N   CA   sing N N 286 
PHE   N   H    sing N N 287 
PHE   N   H2   sing N N 288 
PHE   CA  C    sing N N 289 
PHE   CA  CB   sing N N 290 
PHE   CA  HA   sing N N 291 
PHE   C   O    doub N N 292 
PHE   C   OXT  sing N N 293 
PHE   CB  CG   sing N N 294 
PHE   CB  HB2  sing N N 295 
PHE   CB  HB3  sing N N 296 
PHE   CG  CD1  doub Y N 297 
PHE   CG  CD2  sing Y N 298 
PHE   CD1 CE1  sing Y N 299 
PHE   CD1 HD1  sing N N 300 
PHE   CD2 CE2  doub Y N 301 
PHE   CD2 HD2  sing N N 302 
PHE   CE1 CZ   doub Y N 303 
PHE   CE1 HE1  sing N N 304 
PHE   CE2 CZ   sing Y N 305 
PHE   CE2 HE2  sing N N 306 
PHE   CZ  HZ   sing N N 307 
PHE   OXT HXT  sing N N 308 
PRO   N   CA   sing N N 309 
PRO   N   CD   sing N N 310 
PRO   N   H    sing N N 311 
PRO   CA  C    sing N N 312 
PRO   CA  CB   sing N N 313 
PRO   CA  HA   sing N N 314 
PRO   C   O    doub N N 315 
PRO   C   OXT  sing N N 316 
PRO   CB  CG   sing N N 317 
PRO   CB  HB2  sing N N 318 
PRO   CB  HB3  sing N N 319 
PRO   CG  CD   sing N N 320 
PRO   CG  HG2  sing N N 321 
PRO   CG  HG3  sing N N 322 
PRO   CD  HD2  sing N N 323 
PRO   CD  HD3  sing N N 324 
PRO   OXT HXT  sing N N 325 
SER   N   CA   sing N N 326 
SER   N   H    sing N N 327 
SER   N   H2   sing N N 328 
SER   CA  C    sing N N 329 
SER   CA  CB   sing N N 330 
SER   CA  HA   sing N N 331 
SER   C   O    doub N N 332 
SER   C   OXT  sing N N 333 
SER   CB  OG   sing N N 334 
SER   CB  HB2  sing N N 335 
SER   CB  HB3  sing N N 336 
SER   OG  HG   sing N N 337 
SER   OXT HXT  sing N N 338 
SO4   S   O1   doub N N 339 
SO4   S   O2   doub N N 340 
SO4   S   O3   sing N N 341 
SO4   S   O4   sing N N 342 
THR   N   CA   sing N N 343 
THR   N   H    sing N N 344 
THR   N   H2   sing N N 345 
THR   CA  C    sing N N 346 
THR   CA  CB   sing N N 347 
THR   CA  HA   sing N N 348 
THR   C   O    doub N N 349 
THR   C   OXT  sing N N 350 
THR   CB  OG1  sing N N 351 
THR   CB  CG2  sing N N 352 
THR   CB  HB   sing N N 353 
THR   OG1 HG1  sing N N 354 
THR   CG2 HG21 sing N N 355 
THR   CG2 HG22 sing N N 356 
THR   CG2 HG23 sing N N 357 
THR   OXT HXT  sing N N 358 
TRP   N   CA   sing N N 359 
TRP   N   H    sing N N 360 
TRP   N   H2   sing N N 361 
TRP   CA  C    sing N N 362 
TRP   CA  CB   sing N N 363 
TRP   CA  HA   sing N N 364 
TRP   C   O    doub N N 365 
TRP   C   OXT  sing N N 366 
TRP   CB  CG   sing N N 367 
TRP   CB  HB2  sing N N 368 
TRP   CB  HB3  sing N N 369 
TRP   CG  CD1  doub Y N 370 
TRP   CG  CD2  sing Y N 371 
TRP   CD1 NE1  sing Y N 372 
TRP   CD1 HD1  sing N N 373 
TRP   CD2 CE2  doub Y N 374 
TRP   CD2 CE3  sing Y N 375 
TRP   NE1 CE2  sing Y N 376 
TRP   NE1 HE1  sing N N 377 
TRP   CE2 CZ2  sing Y N 378 
TRP   CE3 CZ3  doub Y N 379 
TRP   CE3 HE3  sing N N 380 
TRP   CZ2 CH2  doub Y N 381 
TRP   CZ2 HZ2  sing N N 382 
TRP   CZ3 CH2  sing Y N 383 
TRP   CZ3 HZ3  sing N N 384 
TRP   CH2 HH2  sing N N 385 
TRP   OXT HXT  sing N N 386 
TYR   N   CA   sing N N 387 
TYR   N   H    sing N N 388 
TYR   N   H2   sing N N 389 
TYR   CA  C    sing N N 390 
TYR   CA  CB   sing N N 391 
TYR   CA  HA   sing N N 392 
TYR   C   O    doub N N 393 
TYR   C   OXT  sing N N 394 
TYR   CB  CG   sing N N 395 
TYR   CB  HB2  sing N N 396 
TYR   CB  HB3  sing N N 397 
TYR   CG  CD1  doub Y N 398 
TYR   CG  CD2  sing Y N 399 
TYR   CD1 CE1  sing Y N 400 
TYR   CD1 HD1  sing N N 401 
TYR   CD2 CE2  doub Y N 402 
TYR   CD2 HD2  sing N N 403 
TYR   CE1 CZ   doub Y N 404 
TYR   CE1 HE1  sing N N 405 
TYR   CE2 CZ   sing Y N 406 
TYR   CE2 HE2  sing N N 407 
TYR   CZ  OH   sing N N 408 
TYR   OH  HH   sing N N 409 
TYR   OXT HXT  sing N N 410 
VAL   N   CA   sing N N 411 
VAL   N   H    sing N N 412 
VAL   N   H2   sing N N 413 
VAL   CA  C    sing N N 414 
VAL   CA  CB   sing N N 415 
VAL   CA  HA   sing N N 416 
VAL   C   O    doub N N 417 
VAL   C   OXT  sing N N 418 
VAL   CB  CG1  sing N N 419 
VAL   CB  CG2  sing N N 420 
VAL   CB  HB   sing N N 421 
VAL   CG1 HG11 sing N N 422 
VAL   CG1 HG12 sing N N 423 
VAL   CG1 HG13 sing N N 424 
VAL   CG2 HG21 sing N N 425 
VAL   CG2 HG22 sing N N 426 
VAL   CG2 HG23 sing N N 427 
VAL   OXT HXT  sing N N 428 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   1 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   2HBT 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8Z35 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   0.013998 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   -0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.013998 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   -0.000000 
_atom_sites.fract_transf_matrix[3][3]   0.021901 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
CL 
FE 
N  
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . HIS   A 1 3   ? 30.279 -1.955  26.128  1.00 34.54  ? 182 HIS   A N   1 
ATOM   2    C  CA  . HIS   A 1 3   ? 31.125 -0.888  26.732  1.00 34.75  ? 182 HIS   A CA  1 
ATOM   3    C  C   . HIS   A 1 3   ? 30.450 0.467   26.534  1.00 32.59  ? 182 HIS   A C   1 
ATOM   4    O  O   . HIS   A 1 3   ? 30.203 0.891   25.404  1.00 31.47  ? 182 HIS   A O   1 
ATOM   5    C  CB  . HIS   A 1 3   ? 32.554 -0.947  26.186  1.00 37.74  ? 182 HIS   A CB  1 
ATOM   6    C  CG  . HIS   A 1 3   ? 33.563 -0.238  27.029  1.00 39.14  ? 182 HIS   A CG  1 
ATOM   7    N  ND1 . HIS   A 1 3   ? 33.726 -0.487  28.376  1.00 41.27  ? 182 HIS   A ND1 1 
ATOM   8    C  CD2 . HIS   A 1 3   ? 34.471 0.696   26.715  1.00 40.68  ? 182 HIS   A CD2 1 
ATOM   9    C  CE1 . HIS   A 1 3   ? 34.698 0.280   28.851  1.00 40.87  ? 182 HIS   A CE1 1 
ATOM   10   N  NE2 . HIS   A 1 3   ? 35.172 1.001   27.856  1.00 39.83  ? 182 HIS   A NE2 1 
ATOM   11   N  N   . HIS   A 1 4   ? 30.193 1.137   27.664  1.00 30.19  ? 183 HIS   A N   1 
ATOM   12   C  CA  . HIS   A 1 4   ? 29.323 2.298   27.758  1.00 29.53  ? 183 HIS   A CA  1 
ATOM   13   C  C   . HIS   A 1 4   ? 29.998 3.547   27.194  1.00 28.70  ? 183 HIS   A C   1 
ATOM   14   O  O   . HIS   A 1 4   ? 29.397 4.621   27.201  1.00 29.08  ? 183 HIS   A O   1 
ATOM   15   C  CB  . HIS   A 1 4   ? 28.897 2.511   29.216  1.00 29.30  ? 183 HIS   A CB  1 
ATOM   16   C  CG  . HIS   A 1 4   ? 30.027 2.855   30.135  1.00 29.64  ? 183 HIS   A CG  1 
ATOM   17   N  ND1 . HIS   A 1 4   ? 30.529 1.968   31.063  1.00 29.87  ? 183 HIS   A ND1 1 
ATOM   18   C  CD2 . HIS   A 1 4   ? 30.761 3.971   30.257  1.00 29.51  ? 183 HIS   A CD2 1 
ATOM   19   C  CE1 . HIS   A 1 4   ? 31.526 2.541   31.723  1.00 29.42  ? 183 HIS   A CE1 1 
ATOM   20   N  NE2 . HIS   A 1 4   ? 31.683 3.758   31.249  1.00 29.84  ? 183 HIS   A NE2 1 
ATOM   21   N  N   . HIS   A 1 5   ? 31.244 3.405   26.719  1.00 26.95  ? 184 HIS   A N   1 
ATOM   22   C  CA  . HIS   A 1 5   ? 31.974 4.522   26.138  1.00 26.07  ? 184 HIS   A CA  1 
ATOM   23   C  C   . HIS   A 1 5   ? 31.631 4.677   24.658  1.00 25.60  ? 184 HIS   A C   1 
ATOM   24   O  O   . HIS   A 1 5   ? 31.993 5.682   24.050  1.00 24.49  ? 184 HIS   A O   1 
ATOM   25   C  CB  . HIS   A 1 5   ? 33.486 4.383   26.354  1.00 24.94  ? 184 HIS   A CB  1 
ATOM   26   C  CG  . HIS   A 1 5   ? 33.916 4.502   27.777  1.00 24.20  ? 184 HIS   A CG  1 
ATOM   27   N  ND1 . HIS   A 1 5   ? 34.668 3.532   28.401  1.00 23.83  ? 184 HIS   A ND1 1 
ATOM   28   C  CD2 . HIS   A 1 5   ? 33.727 5.465   28.690  1.00 24.20  ? 184 HIS   A CD2 1 
ATOM   29   C  CE1 . HIS   A 1 5   ? 34.911 3.901   29.651  1.00 23.64  ? 184 HIS   A CE1 1 
ATOM   30   N  NE2 . HIS   A 1 5   ? 34.347 5.071   29.847  1.00 23.76  ? 184 HIS   A NE2 1 
ATOM   31   N  N   . HIS   A 1 6   ? 30.933 3.679   24.097  1.00 26.05  ? 185 HIS   A N   1 
ATOM   32   C  CA  . HIS   A 1 6   ? 30.559 3.671   22.691  1.00 27.06  ? 185 HIS   A CA  1 
ATOM   33   C  C   . HIS   A 1 6   ? 29.092 4.067   22.533  1.00 27.39  ? 185 HIS   A C   1 
ATOM   34   O  O   . HIS   A 1 6   ? 28.263 3.765   23.390  1.00 26.81  ? 185 HIS   A O   1 
ATOM   35   C  CB  . HIS   A 1 6   ? 30.839 2.306   22.052  1.00 27.94  ? 185 HIS   A CB  1 
ATOM   36   C  CG  . HIS   A 1 6   ? 32.279 1.908   22.063  1.00 28.44  ? 185 HIS   A CG  1 
ATOM   37   N  ND1 . HIS   A 1 6   ? 33.063 1.923   20.930  1.00 28.61  ? 185 HIS   A ND1 1 
ATOM   38   C  CD2 . HIS   A 1 6   ? 33.077 1.503   23.060  1.00 28.48  ? 185 HIS   A CD2 1 
ATOM   39   C  CE1 . HIS   A 1 6   ? 34.290 1.530   21.243  1.00 29.00  ? 185 HIS   A CE1 1 
ATOM   40   N  NE2 . HIS   A 1 6   ? 34.320 1.268   22.531  1.00 28.59  ? 185 HIS   A NE2 1 
ATOM   41   N  N   . HIS   A 1 7   ? 28.788 4.738   21.415  1.00 27.24  ? 186 HIS   A N   1 
ATOM   42   C  CA  . HIS   A 1 7   ? 27.450 5.238   21.137  1.00 27.76  ? 186 HIS   A CA  1 
ATOM   43   C  C   . HIS   A 1 7   ? 27.140 5.050   19.655  1.00 26.59  ? 186 HIS   A C   1 
ATOM   44   O  O   . HIS   A 1 7   ? 28.015 5.218   18.809  1.00 24.47  ? 186 HIS   A O   1 
ATOM   45   C  CB  . HIS   A 1 7   ? 27.327 6.698   21.591  1.00 29.07  ? 186 HIS   A CB  1 
ATOM   46   C  CG  . HIS   A 1 7   ? 27.761 6.906   23.005  1.00 31.33  ? 186 HIS   A CG  1 
ATOM   47   N  ND1 . HIS   A 1 7   ? 27.094 6.361   24.081  1.00 31.91  ? 186 HIS   A ND1 1 
ATOM   48   C  CD2 . HIS   A 1 7   ? 28.806 7.573   23.517  1.00 32.32  ? 186 HIS   A CD2 1 
ATOM   49   C  CE1 . HIS   A 1 7   ? 27.716 6.703   25.201  1.00 31.65  ? 186 HIS   A CE1 1 
ATOM   50   N  NE2 . HIS   A 1 7   ? 28.760 7.437   24.881  1.00 32.11  ? 186 HIS   A NE2 1 
ATOM   51   N  N   . HIS   A 1 8   ? 25.887 4.687   19.355  1.00 26.81  ? 187 HIS   A N   1 
ATOM   52   C  CA  . HIS   A 1 8   ? 25.462 4.448   17.986  1.00 27.45  ? 187 HIS   A CA  1 
ATOM   53   C  C   . HIS   A 1 8   ? 25.389 5.766   17.221  1.00 25.72  ? 187 HIS   A C   1 
ATOM   54   O  O   . HIS   A 1 8   ? 24.867 6.756   17.727  1.00 24.52  ? 187 HIS   A O   1 
ATOM   55   C  CB  . HIS   A 1 8   ? 24.144 3.665   17.944  1.00 30.52  ? 187 HIS   A CB  1 
ATOM   56   C  CG  . HIS   A 1 8   ? 24.350 2.189   17.870  1.00 32.71  ? 187 HIS   A CG  1 
ATOM   57   N  ND1 . HIS   A 1 8   ? 24.746 1.561   16.709  1.00 34.28  ? 187 HIS   A ND1 1 
ATOM   58   C  CD2 . HIS   A 1 8   ? 24.226 1.225   18.790  1.00 34.43  ? 187 HIS   A CD2 1 
ATOM   59   C  CE1 . HIS   A 1 8   ? 24.858 0.259   16.931  1.00 34.99  ? 187 HIS   A CE1 1 
ATOM   60   N  NE2 . HIS   A 1 8   ? 24.546 0.033   18.189  1.00 35.86  ? 187 HIS   A NE2 1 
ATOM   61   N  N   . LEU   A 1 9   ? 25.951 5.758   16.007  1.00 25.10  ? 188 LEU   A N   1 
ATOM   62   C  CA  . LEU   A 1 9   ? 25.701 6.802   15.028  1.00 25.13  ? 188 LEU   A CA  1 
ATOM   63   C  C   . LEU   A 1 9   ? 24.246 6.686   14.584  1.00 24.06  ? 188 LEU   A C   1 
ATOM   64   O  O   . LEU   A 1 9   ? 23.797 5.596   14.235  1.00 23.20  ? 188 LEU   A O   1 
ATOM   65   C  CB  . LEU   A 1 9   ? 26.635 6.592   13.831  1.00 26.02  ? 188 LEU   A CB  1 
ATOM   66   C  CG  . LEU   A 1 9   ? 28.104 6.957   14.040  1.00 26.42  ? 188 LEU   A CG  1 
ATOM   67   C  CD1 . LEU   A 1 9   ? 28.937 6.525   12.844  1.00 27.55  ? 188 LEU   A CD1 1 
ATOM   68   C  CD2 . LEU   A 1 9   ? 28.260 8.451   14.265  1.00 26.87  ? 188 LEU   A CD2 1 
ATOM   69   N  N   . PRO   A 1 10  ? 23.454 7.784   14.599  1.00 23.61  ? 189 PRO   A N   1 
ATOM   70   C  CA  . PRO   A 1 10  ? 22.121 7.763   13.998  1.00 23.02  ? 189 PRO   A CA  1 
ATOM   71   C  C   . PRO   A 1 10  ? 22.215 7.405   12.517  1.00 22.78  ? 189 PRO   A C   1 
ATOM   72   O  O   . PRO   A 1 10  ? 23.237 7.645   11.878  1.00 22.97  ? 189 PRO   A O   1 
ATOM   73   C  CB  . PRO   A 1 10  ? 21.623 9.207   14.167  1.00 22.96  ? 189 PRO   A CB  1 
ATOM   74   C  CG  . PRO   A 1 10  ? 22.416 9.733   15.343  1.00 23.40  ? 189 PRO   A CG  1 
ATOM   75   C  CD  . PRO   A 1 10  ? 23.777 9.079   15.218  1.00 23.28  ? 189 PRO   A CD  1 
ATOM   76   N  N   . ALA   A 1 11  ? 21.125 6.843   11.987  1.00 23.19  ? 190 ALA   A N   1 
ATOM   77   C  CA  . ALA   A 1 11  ? 21.036 6.397   10.606  1.00 23.54  ? 190 ALA   A CA  1 
ATOM   78   C  C   . ALA   A 1 11  ? 21.444 7.509   9.639   1.00 23.58  ? 190 ALA   A C   1 
ATOM   79   O  O   . ALA   A 1 11  ? 22.187 7.255   8.693   1.00 23.33  ? 190 ALA   A O   1 
ATOM   80   C  CB  . ALA   A 1 11  ? 19.639 5.900   10.321  1.00 23.68  ? 190 ALA   A CB  1 
ATOM   81   N  N   . LEU   A 1 12  ? 20.957 8.735   9.884   1.00 22.75  ? 191 LEU   A N   1 
ATOM   82   C  CA  . LEU   A 1 12  ? 21.228 9.865   9.006   1.00 22.94  ? 191 LEU   A CA  1 
ATOM   83   C  C   . LEU   A 1 12  ? 22.729 10.137  8.942   1.00 22.80  ? 191 LEU   A C   1 
ATOM   84   O  O   . LEU   A 1 12  ? 23.273 10.392  7.868   1.00 22.47  ? 191 LEU   A O   1 
ATOM   85   C  CB  . LEU   A 1 12  ? 20.475 11.104  9.506   1.00 23.22  ? 191 LEU   A CB  1 
ATOM   86   C  CG  . LEU   A 1 12  ? 20.771 12.397  8.745   1.00 23.57  ? 191 LEU   A CG  1 
ATOM   87   C  CD1 . LEU   A 1 12  ? 20.135 12.370  7.363   1.00 24.22  ? 191 LEU   A CD1 1 
ATOM   88   C  CD2 . LEU   A 1 12  ? 20.299 13.617  9.526   1.00 23.81  ? 191 LEU   A CD2 1 
ATOM   89   N  N   . LYS   A 1 13  ? 23.380 10.085  10.109  1.00 22.97  ? 192 LYS   A N   1 
ATOM   90   C  CA  . LYS   A 1 13  ? 24.789 10.411  10.245  1.00 23.75  ? 192 LYS   A CA  1 
ATOM   91   C  C   . LYS   A 1 13  ? 25.626 9.351   9.531   1.00 24.50  ? 192 LYS   A C   1 
ATOM   92   O  O   . LYS   A 1 13  ? 26.537 9.679   8.772   1.00 23.85  ? 192 LYS   A O   1 
ATOM   93   C  CB  . LYS   A 1 13  ? 25.140 10.538  11.731  1.00 23.56  ? 192 LYS   A CB  1 
ATOM   94   C  CG  . LYS   A 1 13  ? 26.451 11.242  12.049  1.00 24.86  ? 192 LYS   A CG  1 
ATOM   95   C  CD  . LYS   A 1 13  ? 26.559 11.605  13.520  1.00 25.94  ? 192 LYS   A CD  1 
ATOM   96   C  CE  . LYS   A 1 13  ? 27.868 12.260  13.907  1.00 25.07  ? 192 LYS   A CE  1 
ATOM   97   N  NZ  . LYS   A 1 13  ? 28.027 13.593  13.284  1.00 25.70  ? 192 LYS   A NZ  1 
ATOM   98   N  N   . LEU   A 1 14  ? 25.294 8.078   9.770   1.00 25.86  ? 193 LEU   A N   1 
ATOM   99   C  CA  . LEU   A 1 14  ? 26.024 6.977   9.162   1.00 26.69  ? 193 LEU   A CA  1 
ATOM   100  C  C   . LEU   A 1 14  ? 25.872 7.033   7.642   1.00 27.02  ? 193 LEU   A C   1 
ATOM   101  O  O   . LEU   A 1 14  ? 26.850 6.864   6.916   1.00 26.79  ? 193 LEU   A O   1 
ATOM   102  C  CB  . LEU   A 1 14  ? 25.518 5.654   9.746   1.00 27.71  ? 193 LEU   A CB  1 
ATOM   103  C  CG  . LEU   A 1 14  ? 26.207 4.385   9.241   1.00 28.80  ? 193 LEU   A CG  1 
ATOM   104  C  CD1 . LEU   A 1 14  ? 27.690 4.389   9.588   1.00 28.59  ? 193 LEU   A CD1 1 
ATOM   105  C  CD2 . LEU   A 1 14  ? 25.533 3.148   9.818   1.00 29.13  ? 193 LEU   A CD2 1 
ATOM   106  N  N   . ALA   A 1 15  ? 24.648 7.306   7.176   1.00 26.01  ? 194 ALA   A N   1 
ATOM   107  C  CA  . ALA   A 1 15  ? 24.356 7.376   5.753   1.00 26.59  ? 194 ALA   A CA  1 
ATOM   108  C  C   . ALA   A 1 15  ? 25.193 8.463   5.076   1.00 27.02  ? 194 ALA   A C   1 
ATOM   109  O  O   . ALA   A 1 15  ? 25.871 8.201   4.084   1.00 26.27  ? 194 ALA   A O   1 
ATOM   110  C  CB  . ALA   A 1 15  ? 22.878 7.599   5.539   1.00 27.38  ? 194 ALA   A CB  1 
ATOM   111  N  N   . LEU   A 1 16  ? 25.159 9.679   5.632   1.00 26.63  ? 195 LEU   A N   1 
ATOM   112  C  CA  . LEU   A 1 16  ? 25.679 10.842  4.931   1.00 27.41  ? 195 LEU   A CA  1 
ATOM   113  C  C   . LEU   A 1 16  ? 27.185 10.990  5.132   1.00 28.09  ? 195 LEU   A C   1 
ATOM   114  O  O   . LEU   A 1 16  ? 27.877 11.468  4.235   1.00 27.81  ? 195 LEU   A O   1 
ATOM   115  C  CB  . LEU   A 1 16  ? 24.911 12.092  5.377   1.00 27.00  ? 195 LEU   A CB  1 
ATOM   116  C  CG  . LEU   A 1 16  ? 23.459 12.157  4.908   1.00 27.05  ? 195 LEU   A CG  1 
ATOM   117  C  CD1 . LEU   A 1 16  ? 22.860 13.522  5.189   1.00 26.99  ? 195 LEU   A CD1 1 
ATOM   118  C  CD2 . LEU   A 1 16  ? 23.351 11.832  3.425   1.00 27.84  ? 195 LEU   A CD2 1 
ATOM   119  N  N   . GLU   A 1 17  ? 27.686 10.574  6.301   1.00 28.29  ? 196 GLU   A N   1 
ATOM   120  C  CA  . GLU   A 1 17  ? 29.094 10.749  6.623   1.00 29.30  ? 196 GLU   A CA  1 
ATOM   121  C  C   . GLU   A 1 17  ? 29.924 9.566   6.126   1.00 29.03  ? 196 GLU   A C   1 
ATOM   122  O  O   . GLU   A 1 17  ? 31.147 9.665   6.074   1.00 28.28  ? 196 GLU   A O   1 
ATOM   123  C  CB  . GLU   A 1 17  ? 29.315 10.946  8.126   1.00 30.10  ? 196 GLU   A CB  1 
ATOM   124  C  CG  . GLU   A 1 17  ? 28.761 12.254  8.663   1.00 31.84  ? 196 GLU   A CG  1 
ATOM   125  C  CD  . GLU   A 1 17  ? 29.068 12.530  10.126  1.00 33.29  ? 196 GLU   A CD  1 
ATOM   126  O  OE1 . GLU   A 1 17  ? 29.832 11.748  10.730  1.00 34.31  ? 196 GLU   A OE1 1 
ATOM   127  O  OE2 . GLU   A 1 17  ? 28.531 13.518  10.664  1.00 33.38  ? 196 GLU   A OE2 1 
ATOM   128  N  N   . TYR   A 1 18  ? 29.272 8.448   5.776   1.00 28.29  ? 197 TYR   A N   1 
ATOM   129  C  CA  . TYR   A 1 18  ? 30.040 7.253   5.462   1.00 28.03  ? 197 TYR   A CA  1 
ATOM   130  C  C   . TYR   A 1 18  ? 29.487 6.494   4.254   1.00 27.49  ? 197 TYR   A C   1 
ATOM   131  O  O   . TYR   A 1 18  ? 30.198 6.317   3.268   1.00 27.07  ? 197 TYR   A O   1 
ATOM   132  C  CB  . TYR   A 1 18  ? 30.230 6.360   6.692   1.00 29.54  ? 197 TYR   A CB  1 
ATOM   133  C  CG  . TYR   A 1 18  ? 31.229 5.253   6.471   1.00 31.25  ? 197 TYR   A CG  1 
ATOM   134  C  CD1 . TYR   A 1 18  ? 32.578 5.536   6.310   1.00 31.50  ? 197 TYR   A CD1 1 
ATOM   135  C  CD2 . TYR   A 1 18  ? 30.826 3.930   6.376   1.00 31.20  ? 197 TYR   A CD2 1 
ATOM   136  C  CE1 . TYR   A 1 18  ? 33.506 4.533   6.087   1.00 32.54  ? 197 TYR   A CE1 1 
ATOM   137  C  CE2 . TYR   A 1 18  ? 31.743 2.914   6.153   1.00 32.40  ? 197 TYR   A CE2 1 
ATOM   138  C  CZ  . TYR   A 1 18  ? 33.085 3.217   6.002   1.00 34.05  ? 197 TYR   A CZ  1 
ATOM   139  O  OH  . TYR   A 1 18  ? 34.002 2.217   5.786   1.00 37.54  ? 197 TYR   A OH  1 
ATOM   140  N  N   . ILE   A 1 19  ? 28.237 6.023   4.342   1.00 26.06  ? 198 ILE   A N   1 
ATOM   141  C  CA  . ILE   A 1 19  ? 27.706 5.118   3.331   1.00 26.12  ? 198 ILE   A CA  1 
ATOM   142  C  C   . ILE   A 1 19  ? 27.686 5.806   1.965   1.00 26.08  ? 198 ILE   A C   1 
ATOM   143  O  O   . ILE   A 1 19  ? 28.192 5.252   0.991   1.00 25.89  ? 198 ILE   A O   1 
ATOM   144  C  CB  . ILE   A 1 19  ? 26.336 4.532   3.735   1.00 25.11  ? 198 ILE   A CB  1 
ATOM   145  C  CG1 . ILE   A 1 19  ? 26.435 3.714   5.027   1.00 25.61  ? 198 ILE   A CG1 1 
ATOM   146  C  CG2 . ILE   A 1 19  ? 25.744 3.706   2.598   1.00 24.17  ? 198 ILE   A CG2 1 
ATOM   147  C  CD1 . ILE   A 1 19  ? 25.106 3.210   5.545   1.00 26.13  ? 198 ILE   A CD1 1 
ATOM   148  N  N   . VAL   A 1 20  ? 27.110 7.013   1.904   1.00 26.31  ? 199 VAL   A N   1 
ATOM   149  C  CA  . VAL   A 1 20  ? 26.949 7.728   0.644   1.00 26.80  ? 199 VAL   A CA  1 
ATOM   150  C  C   . VAL   A 1 20  ? 28.307 7.976   -0.016  1.00 27.63  ? 199 VAL   A C   1 
ATOM   151  O  O   . VAL   A 1 20  ? 28.498 7.571   -1.161  1.00 27.76  ? 199 VAL   A O   1 
ATOM   152  C  CB  . VAL   A 1 20  ? 26.098 9.007   0.790   1.00 26.64  ? 199 VAL   A CB  1 
ATOM   153  C  CG1 . VAL   A 1 20  ? 26.258 9.951   -0.394  1.00 27.17  ? 199 VAL   A CG1 1 
ATOM   154  C  CG2 . VAL   A 1 20  ? 24.630 8.672   1.009   1.00 26.60  ? 199 VAL   A CG2 1 
ATOM   155  N  N   . PRO   A 1 21  ? 29.287 8.639   0.649   1.00 28.73  ? 200 PRO   A N   1 
ATOM   156  C  CA  . PRO   A 1 21  ? 30.599 8.865   0.038   1.00 29.46  ? 200 PRO   A CA  1 
ATOM   157  C  C   . PRO   A 1 21  ? 31.304 7.562   -0.334  1.00 29.66  ? 200 PRO   A C   1 
ATOM   158  O  O   . PRO   A 1 21  ? 31.863 7.451   -1.421  1.00 28.66  ? 200 PRO   A O   1 
ATOM   159  C  CB  . PRO   A 1 21  ? 31.403 9.651   1.088   1.00 29.45  ? 200 PRO   A CB  1 
ATOM   160  C  CG  . PRO   A 1 21  ? 30.632 9.484   2.384   1.00 29.61  ? 200 PRO   A CG  1 
ATOM   161  C  CD  . PRO   A 1 21  ? 29.189 9.242   1.989   1.00 29.17  ? 200 PRO   A CD  1 
ATOM   162  N  N   . CYS   A 1 22  ? 31.237 6.573   0.567   1.00 30.10  ? 201 CYS   A N   1 
ATOM   163  C  CA  . CYS   A 1 22  ? 31.906 5.297   0.379   1.00 30.67  ? 201 CYS   A CA  1 
ATOM   164  C  C   . CYS   A 1 22  ? 31.376 4.595   -0.871  1.00 29.91  ? 201 CYS   A C   1 
ATOM   165  O  O   . CYS   A 1 22  ? 32.155 4.040   -1.646  1.00 29.79  ? 201 CYS   A O   1 
ATOM   166  C  CB  . CYS   A 1 22  ? 31.718 4.410   1.604   1.00 34.90  ? 201 CYS   A CB  1 
ATOM   167  S  SG  . CYS   A 1 22  ? 33.051 3.206   1.830   1.00 43.16  ? 201 CYS   A SG  1 
ATOM   168  N  N   . MET   A 1 23  ? 30.052 4.651   -1.073  1.00 29.23  ? 202 MET   A N   1 
ATOM   169  C  CA  . MET   A 1 23  ? 29.397 3.974   -2.184  1.00 28.83  ? 202 MET   A CA  1 
ATOM   170  C  C   . MET   A 1 23  ? 29.707 4.685   -3.502  1.00 28.79  ? 202 MET   A C   1 
ATOM   171  O  O   . MET   A 1 23  ? 30.015 4.036   -4.501  1.00 28.03  ? 202 MET   A O   1 
ATOM   172  C  CB  . MET   A 1 23  ? 27.879 3.894   -1.976  1.00 27.99  ? 202 MET   A CB  1 
ATOM   173  C  CG  . MET   A 1 23  ? 27.456 2.808   -0.989  1.00 26.93  ? 202 MET   A CG  1 
ATOM   174  S  SD  . MET   A 1 23  ? 27.847 1.113   -1.510  1.00 25.93  ? 202 MET   A SD  1 
ATOM   175  C  CE  . MET   A 1 23  ? 26.735 0.919   -2.903  1.00 25.43  ? 202 MET   A CE  1 
ATOM   176  N  N   . ASN   A 1 24  ? 29.646 6.022   -3.498  1.00 29.45  ? 203 ASN   A N   1 
ATOM   177  C  CA  . ASN   A 1 24  ? 29.873 6.791   -4.713  1.00 30.39  ? 203 ASN   A CA  1 
ATOM   178  C  C   . ASN   A 1 24  ? 31.332 6.693   -5.159  1.00 30.78  ? 203 ASN   A C   1 
ATOM   179  O  O   . ASN   A 1 24  ? 31.619 6.842   -6.346  1.00 31.18  ? 203 ASN   A O   1 
ATOM   180  C  CB  . ASN   A 1 24  ? 29.398 8.242   -4.597  1.00 30.59  ? 203 ASN   A CB  1 
ATOM   181  C  CG  . ASN   A 1 24  ? 27.890 8.377   -4.553  1.00 31.10  ? 203 ASN   A CG  1 
ATOM   182  O  OD1 . ASN   A 1 24  ? 27.179 7.708   -5.301  1.00 30.71  ? 203 ASN   A OD1 1 
ATOM   183  N  ND2 . ASN   A 1 24  ? 27.391 9.234   -3.676  1.00 31.12  ? 203 ASN   A ND2 1 
ATOM   184  N  N   . LYS   A 1 25  ? 32.242 6.437   -4.210  1.00 30.39  ? 204 LYS   A N   1 
ATOM   185  C  CA  . LYS   A 1 25  ? 33.667 6.389   -4.502  1.00 31.07  ? 204 LYS   A CA  1 
ATOM   186  C  C   . LYS   A 1 25  ? 34.117 4.968   -4.841  1.00 29.74  ? 204 LYS   A C   1 
ATOM   187  O  O   . LYS   A 1 25  ? 34.891 4.778   -5.778  1.00 27.84  ? 204 LYS   A O   1 
ATOM   188  C  CB  . LYS   A 1 25  ? 34.494 6.971   -3.350  1.00 33.83  ? 204 LYS   A CB  1 
ATOM   189  C  CG  . LYS   A 1 25  ? 34.448 8.490   -3.211  1.00 38.18  ? 204 LYS   A CG  1 
ATOM   190  C  CD  . LYS   A 1 25  ? 35.365 9.053   -2.135  1.00 40.51  ? 204 LYS   A CD  1 
ATOM   191  C  CE  . LYS   A 1 25  ? 34.901 8.766   -0.721  1.00 42.30  ? 204 LYS   A CE  1 
ATOM   192  N  NZ  . LYS   A 1 25  ? 35.784 9.391   0.294   1.00 44.05  ? 204 LYS   A NZ  1 
ATOM   193  N  N   . HIS   A 1 26  ? 33.639 3.977   -4.075  1.00 28.47  ? 205 HIS   A N   1 
ATOM   194  C  CA  . HIS   A 1 26  ? 34.203 2.636   -4.123  1.00 28.65  ? 205 HIS   A CA  1 
ATOM   195  C  C   . HIS   A 1 26  ? 33.173 1.605   -4.583  1.00 27.17  ? 205 HIS   A C   1 
ATOM   196  O  O   . HIS   A 1 26  ? 33.543 0.509   -5.001  1.00 26.79  ? 205 HIS   A O   1 
ATOM   197  C  CB  . HIS   A 1 26  ? 34.805 2.249   -2.767  1.00 30.88  ? 205 HIS   A CB  1 
ATOM   198  C  CG  . HIS   A 1 26  ? 35.822 3.215   -2.255  1.00 34.54  ? 205 HIS   A CG  1 
ATOM   199  N  ND1 . HIS   A 1 26  ? 36.912 3.623   -2.995  1.00 36.39  ? 205 HIS   A ND1 1 
ATOM   200  C  CD2 . HIS   A 1 26  ? 35.904 3.861   -1.084  1.00 35.68  ? 205 HIS   A CD2 1 
ATOM   201  C  CE1 . HIS   A 1 26  ? 37.628 4.483   -2.280  1.00 37.75  ? 205 HIS   A CE1 1 
ATOM   202  N  NE2 . HIS   A 1 26  ? 37.033 4.640   -1.115  1.00 37.19  ? 205 HIS   A NE2 1 
ATOM   203  N  N   . GLY   A 1 27  ? 31.885 1.951   -4.487  1.00 26.48  ? 206 GLY   A N   1 
ATOM   204  C  CA  . GLY   A 1 27  ? 30.815 1.053   -4.896  1.00 26.46  ? 206 GLY   A CA  1 
ATOM   205  C  C   . GLY   A 1 27  ? 30.614 -0.102  -3.915  1.00 26.21  ? 206 GLY   A C   1 
ATOM   206  O  O   . GLY   A 1 27  ? 29.842 -1.019  -4.189  1.00 25.82  ? 206 GLY   A O   1 
ATOM   207  N  N   . ILE   A 1 28  ? 31.322 -0.031  -2.779  1.00 24.73  ? 207 ILE   A N   1 
ATOM   208  C  CA  . ILE   A 1 28  ? 31.311 -1.031  -1.721  1.00 25.68  ? 207 ILE   A CA  1 
ATOM   209  C  C   . ILE   A 1 28  ? 31.435 -0.282  -0.395  1.00 25.48  ? 207 ILE   A C   1 
ATOM   210  O  O   . ILE   A 1 28  ? 32.207 0.671   -0.304  1.00 25.43  ? 207 ILE   A O   1 
ATOM   211  C  CB  . ILE   A 1 28  ? 32.479 -2.027  -1.899  1.00 25.99  ? 207 ILE   A CB  1 
ATOM   212  C  CG1 . ILE   A 1 28  ? 32.410 -2.785  -3.229  1.00 26.34  ? 207 ILE   A CG1 1 
ATOM   213  C  CG2 . ILE   A 1 28  ? 32.563 -2.985  -0.714  1.00 26.15  ? 207 ILE   A CG2 1 
ATOM   214  C  CD1 . ILE   A 1 28  ? 33.683 -3.521  -3.587  1.00 27.49  ? 207 ILE   A CD1 1 
ATOM   215  N  N   . CYS   A 1 29  ? 30.680 -0.722  0.622   1.00 25.25  ? 208 CYS   A N   1 
ATOM   216  C  CA  . CYS   A 1 29  ? 30.711 -0.088  1.932   1.00 25.71  ? 208 CYS   A CA  1 
ATOM   217  C  C   . CYS   A 1 29  ? 30.460 -1.115  3.034   1.00 25.07  ? 208 CYS   A C   1 
ATOM   218  O  O   . CYS   A 1 29  ? 29.434 -1.793  3.038   1.00 25.13  ? 208 CYS   A O   1 
ATOM   219  C  CB  . CYS   A 1 29  ? 29.678 1.031   2.031   1.00 25.47  ? 208 CYS   A CB  1 
ATOM   220  S  SG  . CYS   A 1 29  ? 29.691 1.859   3.644   1.00 27.16  ? 208 CYS   A SG  1 
ATOM   221  N  N   . VAL   A 1 30  ? 31.407 -1.200  3.975   1.00 24.89  ? 209 VAL   A N   1 
ATOM   222  C  CA  . VAL   A 1 30  ? 31.339 -2.127  5.094   1.00 25.83  ? 209 VAL   A CA  1 
ATOM   223  C  C   . VAL   A 1 30  ? 31.033 -1.336  6.362   1.00 25.97  ? 209 VAL   A C   1 
ATOM   224  O  O   . VAL   A 1 30  ? 31.714 -0.356  6.660   1.00 24.33  ? 209 VAL   A O   1 
ATOM   225  C  CB  . VAL   A 1 30  ? 32.652 -2.922  5.248   1.00 27.60  ? 209 VAL   A CB  1 
ATOM   226  C  CG1 . VAL   A 1 30  ? 32.655 -3.793  6.499   1.00 27.60  ? 209 VAL   A CG1 1 
ATOM   227  C  CG2 . VAL   A 1 30  ? 32.968 -3.754  4.013   1.00 28.15  ? 209 VAL   A CG2 1 
ATOM   228  N  N   . VAL   A 1 31  ? 30.015 -1.791  7.106   1.00 26.24  ? 210 VAL   A N   1 
ATOM   229  C  CA  . VAL   A 1 31  ? 29.630 -1.187  8.372   1.00 26.77  ? 210 VAL   A CA  1 
ATOM   230  C  C   . VAL   A 1 31  ? 29.621 -2.267  9.452   1.00 27.49  ? 210 VAL   A C   1 
ATOM   231  O  O   . VAL   A 1 31  ? 28.774 -3.162  9.433   1.00 27.64  ? 210 VAL   A O   1 
ATOM   232  C  CB  . VAL   A 1 31  ? 28.267 -0.471  8.271   1.00 27.24  ? 210 VAL   A CB  1 
ATOM   233  C  CG1 . VAL   A 1 31  ? 27.827 0.102   9.610   1.00 28.34  ? 210 VAL   A CG1 1 
ATOM   234  C  CG2 . VAL   A 1 31  ? 28.258 0.612   7.200   1.00 26.51  ? 210 VAL   A CG2 1 
ATOM   235  N  N   . ASP   A 1 32  ? 30.568 -2.170  10.395  1.00 27.14  ? 211 ASP   A N   1 
ATOM   236  C  CA  . ASP   A 1 32  ? 30.640 -3.108  11.504  1.00 27.64  ? 211 ASP   A CA  1 
ATOM   237  C  C   . ASP   A 1 32  ? 29.790 -2.609  12.672  1.00 27.63  ? 211 ASP   A C   1 
ATOM   238  O  O   . ASP   A 1 32  ? 29.476 -1.423  12.754  1.00 26.27  ? 211 ASP   A O   1 
ATOM   239  C  CB  . ASP   A 1 32  ? 32.085 -3.431  11.899  1.00 29.46  ? 211 ASP   A CB  1 
ATOM   240  C  CG  . ASP   A 1 32  ? 32.752 -4.453  10.991  1.00 31.38  ? 211 ASP   A CG  1 
ATOM   241  O  OD1 . ASP   A 1 32  ? 32.163 -5.532  10.789  1.00 31.73  ? 211 ASP   A OD1 1 
ATOM   242  O  OD2 . ASP   A 1 32  ? 33.864 -4.173  10.510  1.00 32.74  ? 211 ASP   A OD2 1 
ATOM   243  N  N   . ASP   A 1 33  ? 29.412 -3.548  13.551  1.00 27.91  ? 212 ASP   A N   1 
ATOM   244  C  CA  . ASP   A 1 33  ? 28.697 -3.286  14.792  1.00 29.73  ? 212 ASP   A CA  1 
ATOM   245  C  C   . ASP   A 1 33  ? 27.363 -2.596  14.518  1.00 29.69  ? 212 ASP   A C   1 
ATOM   246  O  O   . ASP   A 1 33  ? 27.004 -1.642  15.206  1.00 29.67  ? 212 ASP   A O   1 
ATOM   247  C  CB  . ASP   A 1 33  ? 29.565 -2.527  15.801  1.00 32.26  ? 212 ASP   A CB  1 
ATOM   248  C  CG  . ASP   A 1 33  ? 30.876 -3.227  16.099  1.00 34.06  ? 212 ASP   A CG  1 
ATOM   249  O  OD1 . ASP   A 1 33  ? 30.844 -4.446  16.348  1.00 36.07  ? 212 ASP   A OD1 1 
ATOM   250  O  OD2 . ASP   A 1 33  ? 31.915 -2.546  16.082  1.00 37.04  ? 212 ASP   A OD2 1 
ATOM   251  N  N   . PHE   A 1 34  ? 26.617 -3.121  13.537  1.00 28.85  ? 213 PHE   A N   1 
ATOM   252  C  CA  . PHE   A 1 34  ? 25.421 -2.452  13.053  1.00 28.67  ? 213 PHE   A CA  1 
ATOM   253  C  C   . PHE   A 1 34  ? 24.328 -2.442  14.121  1.00 29.02  ? 213 PHE   A C   1 
ATOM   254  O  O   . PHE   A 1 34  ? 23.748 -1.391  14.387  1.00 29.24  ? 213 PHE   A O   1 
ATOM   255  C  CB  . PHE   A 1 34  ? 24.944 -3.045  11.723  1.00 27.31  ? 213 PHE   A CB  1 
ATOM   256  C  CG  . PHE   A 1 34  ? 23.690 -2.422  11.161  1.00 26.01  ? 213 PHE   A CG  1 
ATOM   257  C  CD1 . PHE   A 1 34  ? 23.518 -1.044  11.151  1.00 25.71  ? 213 PHE   A CD1 1 
ATOM   258  C  CD2 . PHE   A 1 34  ? 22.686 -3.213  10.619  1.00 25.46  ? 213 PHE   A CD2 1 
ATOM   259  C  CE1 . PHE   A 1 34  ? 22.362 -0.474  10.637  1.00 25.58  ? 213 PHE   A CE1 1 
ATOM   260  C  CE2 . PHE   A 1 34  ? 21.533 -2.641  10.100  1.00 25.11  ? 213 PHE   A CE2 1 
ATOM   261  C  CZ  . PHE   A 1 34  ? 21.375 -1.274  10.105  1.00 25.09  ? 213 PHE   A CZ  1 
ATOM   262  N  N   . LEU   A 1 35  ? 24.058 -3.608  14.724  1.00 27.87  ? 214 LEU   A N   1 
ATOM   263  C  CA  . LEU   A 1 35  ? 22.887 -3.767  15.574  1.00 29.15  ? 214 LEU   A CA  1 
ATOM   264  C  C   . LEU   A 1 35  ? 23.283 -3.993  17.033  1.00 29.16  ? 214 LEU   A C   1 
ATOM   265  O  O   . LEU   A 1 35  ? 22.470 -3.773  17.926  1.00 28.95  ? 214 LEU   A O   1 
ATOM   266  C  CB  . LEU   A 1 35  ? 22.033 -4.931  15.056  1.00 28.37  ? 214 LEU   A CB  1 
ATOM   267  C  CG  . LEU   A 1 35  ? 21.330 -4.716  13.715  1.00 27.81  ? 214 LEU   A CG  1 
ATOM   268  C  CD1 . LEU   A 1 35  ? 20.380 -5.869  13.425  1.00 26.80  ? 214 LEU   A CD1 1 
ATOM   269  C  CD2 . LEU   A 1 35  ? 20.578 -3.395  13.689  1.00 28.60  ? 214 LEU   A CD2 1 
ATOM   270  N  N   . GLY   A 1 36  ? 24.517 -4.456  17.264  1.00 29.95  ? 215 GLY   A N   1 
ATOM   271  C  CA  . GLY   A 1 36  ? 24.973 -4.785  18.606  1.00 30.32  ? 215 GLY   A CA  1 
ATOM   272  C  C   . GLY   A 1 36  ? 24.818 -6.273  18.908  1.00 31.52  ? 215 GLY   A C   1 
ATOM   273  O  O   . GLY   A 1 36  ? 24.105 -6.982  18.201  1.00 31.77  ? 215 GLY   A O   1 
ATOM   274  N  N   . LYS   A 1 37  ? 25.465 -6.716  19.992  1.00 32.50  ? 216 LYS   A N   1 
ATOM   275  C  CA  . LYS   A 1 37  ? 25.643 -8.124  20.315  1.00 34.47  ? 216 LYS   A CA  1 
ATOM   276  C  C   . LYS   A 1 37  ? 24.305 -8.810  20.594  1.00 34.80  ? 216 LYS   A C   1 
ATOM   277  O  O   . LYS   A 1 37  ? 24.084 -9.929  20.130  1.00 34.87  ? 216 LYS   A O   1 
ATOM   278  C  CB  . LYS   A 1 37  ? 26.627 -8.277  21.479  1.00 36.75  ? 216 LYS   A CB  1 
ATOM   279  C  CG  . LYS   A 1 37  ? 26.937 -9.709  21.903  1.00 39.40  ? 216 LYS   A CG  1 
ATOM   280  C  CD  . LYS   A 1 37  ? 28.258 -9.866  22.640  1.00 41.18  ? 216 LYS   A CD  1 
ATOM   281  C  CE  . LYS   A 1 37  ? 28.352 -9.080  23.930  1.00 44.24  ? 216 LYS   A CE  1 
ATOM   282  N  NZ  . LYS   A 1 37  ? 29.651 -9.302  24.610  1.00 45.97  ? 216 LYS   A NZ  1 
ATOM   283  N  N   . GLU   A 1 38  ? 23.425 -8.148  21.358  1.00 34.74  ? 217 GLU   A N   1 
ATOM   284  C  CA  . GLU   A 1 38  ? 22.179 -8.768  21.787  1.00 34.51  ? 217 GLU   A CA  1 
ATOM   285  C  C   . GLU   A 1 38  ? 21.277 -9.037  20.583  1.00 33.25  ? 217 GLU   A C   1 
ATOM   286  O  O   . GLU   A 1 38  ? 20.814 -10.160 20.396  1.00 32.79  ? 217 GLU   A O   1 
ATOM   287  C  CB  . GLU   A 1 38  ? 21.452 -7.932  22.844  1.00 37.40  ? 217 GLU   A CB  1 
ATOM   288  C  CG  . GLU   A 1 38  ? 20.080 -8.492  23.188  1.00 39.98  ? 217 GLU   A CG  1 
ATOM   289  C  CD  . GLU   A 1 38  ? 19.317 -7.812  24.311  1.00 42.44  ? 217 GLU   A CD  1 
ATOM   290  O  OE1 . GLU   A 1 38  ? 18.915 -8.521  25.253  1.00 43.37  ? 217 GLU   A OE1 1 
ATOM   291  O  OE2 . GLU   A 1 38  ? 19.112 -6.583  24.235  1.00 43.99  ? 217 GLU   A OE2 1 
ATOM   292  N  N   . THR   A 1 39  ? 21.029 -7.993  19.783  1.00 32.21  ? 218 THR   A N   1 
ATOM   293  C  CA  . THR   A 1 39  ? 20.178 -8.099  18.608  1.00 31.67  ? 218 THR   A CA  1 
ATOM   294  C  C   . THR   A 1 39  ? 20.786 -9.099  17.625  1.00 30.73  ? 218 THR   A C   1 
ATOM   295  O  O   . THR   A 1 39  ? 20.070 -9.912  17.044  1.00 30.89  ? 218 THR   A O   1 
ATOM   296  C  CB  . THR   A 1 39  ? 19.929 -6.720  17.982  1.00 32.28  ? 218 THR   A CB  1 
ATOM   297  O  OG1 . THR   A 1 39  ? 19.359 -5.874  18.982  1.00 31.61  ? 218 THR   A OG1 1 
ATOM   298  C  CG2 . THR   A 1 39  ? 19.004 -6.764  16.785  1.00 31.59  ? 218 THR   A CG2 1 
ATOM   299  N  N   . GLY   A 1 40  ? 22.113 -9.033  17.462  1.00 31.01  ? 219 GLY   A N   1 
ATOM   300  C  CA  . GLY   A 1 40  ? 22.842 -9.904  16.553  1.00 31.93  ? 219 GLY   A CA  1 
ATOM   301  C  C   . GLY   A 1 40  ? 22.693 -11.378 16.924  1.00 32.32  ? 219 GLY   A C   1 
ATOM   302  O  O   . GLY   A 1 40  ? 22.530 -12.228 16.049  1.00 30.52  ? 219 GLY   A O   1 
ATOM   303  N  N   . GLN   A 1 41  ? 22.749 -11.661 18.232  1.00 32.64  ? 220 GLN   A N   1 
ATOM   304  C  CA  . GLN   A 1 41  ? 22.640 -13.017 18.743  1.00 34.07  ? 220 GLN   A CA  1 
ATOM   305  C  C   . GLN   A 1 41  ? 21.222 -13.539 18.522  1.00 32.90  ? 220 GLN   A C   1 
ATOM   306  O  O   . GLN   A 1 41  ? 21.042 -14.698 18.154  1.00 32.33  ? 220 GLN   A O   1 
ATOM   307  C  CB  . GLN   A 1 41  ? 23.032 -13.067 20.222  1.00 38.42  ? 220 GLN   A CB  1 
ATOM   308  C  CG  . GLN   A 1 41  ? 23.167 -14.481 20.774  1.00 43.57  ? 220 GLN   A CG  1 
ATOM   309  C  CD  . GLN   A 1 41  ? 24.368 -15.221 20.233  1.00 47.97  ? 220 GLN   A CD  1 
ATOM   310  O  OE1 . GLN   A 1 41  ? 25.293 -14.630 19.678  1.00 51.36  ? 220 GLN   A OE1 1 
ATOM   311  N  NE2 . GLN   A 1 41  ? 24.370 -16.532 20.409  1.00 49.88  ? 220 GLN   A NE2 1 
ATOM   312  N  N   . GLN   A 1 42  ? 20.229 -12.666 18.744  1.00 31.53  ? 221 GLN   A N   1 
ATOM   313  C  CA  . GLN   A 1 42  ? 18.826 -13.001 18.559  1.00 32.12  ? 221 GLN   A CA  1 
ATOM   314  C  C   . GLN   A 1 42  ? 18.560 -13.342 17.093  1.00 30.59  ? 221 GLN   A C   1 
ATOM   315  O  O   . GLN   A 1 42  ? 17.803 -14.267 16.803  1.00 29.03  ? 221 GLN   A O   1 
ATOM   316  C  CB  . GLN   A 1 42  ? 17.922 -11.864 19.040  1.00 35.68  ? 221 GLN   A CB  1 
ATOM   317  C  CG  . GLN   A 1 42  ? 17.994 -11.614 20.541  1.00 40.83  ? 221 GLN   A CG  1 
ATOM   318  C  CD  . GLN   A 1 42  ? 16.937 -10.651 21.027  1.00 44.06  ? 221 GLN   A CD  1 
ATOM   319  O  OE1 . GLN   A 1 42  ? 17.220 -9.501  21.355  1.00 45.93  ? 221 GLN   A OE1 1 
ATOM   320  N  NE2 . GLN   A 1 42  ? 15.700 -11.118 21.072  1.00 46.56  ? 221 GLN   A NE2 1 
ATOM   321  N  N   . ILE   A 1 43  ? 19.188 -12.587 16.180  1.00 29.67  ? 222 ILE   A N   1 
ATOM   322  C  CA  . ILE   A 1 43  ? 19.123 -12.861 14.751  1.00 28.71  ? 222 ILE   A CA  1 
ATOM   323  C  C   . ILE   A 1 43  ? 19.661 -14.267 14.500  1.00 28.73  ? 222 ILE   A C   1 
ATOM   324  O  O   . ILE   A 1 43  ? 19.019 -15.067 13.823  1.00 29.57  ? 222 ILE   A O   1 
ATOM   325  C  CB  . ILE   A 1 43  ? 19.922 -11.815 13.943  1.00 29.91  ? 222 ILE   A CB  1 
ATOM   326  C  CG1 . ILE   A 1 43  ? 19.391 -10.390 14.131  1.00 30.65  ? 222 ILE   A CG1 1 
ATOM   327  C  CG2 . ILE   A 1 43  ? 19.990 -12.203 12.470  1.00 28.50  ? 222 ILE   A CG2 1 
ATOM   328  C  CD1 . ILE   A 1 43  ? 18.155 -10.076 13.337  1.00 32.73  ? 222 ILE   A CD1 1 
ATOM   329  N  N   . GLY   A 1 44  ? 20.850 -14.542 15.054  1.00 28.24  ? 223 GLY   A N   1 
ATOM   330  C  CA  . GLY   A 1 44  ? 21.500 -15.836 14.938  1.00 27.76  ? 223 GLY   A CA  1 
ATOM   331  C  C   . GLY   A 1 44  ? 20.590 -16.973 15.394  1.00 28.10  ? 223 GLY   A C   1 
ATOM   332  O  O   . GLY   A 1 44  ? 20.532 -18.018 14.750  1.00 27.90  ? 223 GLY   A O   1 
ATOM   333  N  N   . ASP   A 1 45  ? 19.876 -16.741 16.502  1.00 28.69  ? 224 ASP   A N   1 
ATOM   334  C  CA  . ASP   A 1 45  ? 18.946 -17.711 17.062  1.00 28.60  ? 224 ASP   A CA  1 
ATOM   335  C  C   . ASP   A 1 45  ? 17.822 -17.995 16.067  1.00 27.71  ? 224 ASP   A C   1 
ATOM   336  O  O   . ASP   A 1 45  ? 17.491 -19.152 15.815  1.00 27.99  ? 224 ASP   A O   1 
ATOM   337  C  CB  . ASP   A 1 45  ? 18.420 -17.244 18.423  1.00 30.00  ? 224 ASP   A CB  1 
ATOM   338  C  CG  . ASP   A 1 45  ? 19.475 -17.229 19.518  1.00 31.74  ? 224 ASP   A CG  1 
ATOM   339  O  OD1 . ASP   A 1 45  ? 20.536 -17.859 19.328  1.00 32.17  ? 224 ASP   A OD1 1 
ATOM   340  O  OD2 . ASP   A 1 45  ? 19.232 -16.574 20.553  1.00 33.04  ? 224 ASP   A OD2 1 
ATOM   341  N  N   . GLU   A 1 46  ? 17.249 -16.927 15.499  1.00 26.85  ? 225 GLU   A N   1 
ATOM   342  C  CA  . GLU   A 1 46  ? 16.119 -17.041 14.589  1.00 26.70  ? 225 GLU   A CA  1 
ATOM   343  C  C   . GLU   A 1 46  ? 16.538 -17.782 13.321  1.00 26.47  ? 225 GLU   A C   1 
ATOM   344  O  O   . GLU   A 1 46  ? 15.777 -18.593 12.797  1.00 26.58  ? 225 GLU   A O   1 
ATOM   345  C  CB  . GLU   A 1 46  ? 15.548 -15.661 14.258  1.00 27.42  ? 225 GLU   A CB  1 
ATOM   346  C  CG  . GLU   A 1 46  ? 14.933 -14.959 15.459  1.00 29.00  ? 225 GLU   A CG  1 
ATOM   347  C  CD  . GLU   A 1 46  ? 14.267 -13.625 15.162  1.00 29.51  ? 225 GLU   A CD  1 
ATOM   348  O  OE1 . GLU   A 1 46  ? 14.331 -13.168 14.004  1.00 29.72  ? 225 GLU   A OE1 1 
ATOM   349  O  OE2 . GLU   A 1 46  ? 13.679 -13.045 16.093  1.00 30.13  ? 225 GLU   A OE2 1 
ATOM   350  N  N   . VAL   A 1 47  ? 17.752 -17.493 12.839  1.00 25.66  ? 226 VAL   A N   1 
ATOM   351  C  CA  . VAL   A 1 47  ? 18.245 -18.075 11.601  1.00 26.35  ? 226 VAL   A CA  1 
ATOM   352  C  C   . VAL   A 1 47  ? 18.518 -19.563 11.815  1.00 26.61  ? 226 VAL   A C   1 
ATOM   353  O  O   . VAL   A 1 47  ? 18.207 -20.379 10.948  1.00 26.37  ? 226 VAL   A O   1 
ATOM   354  C  CB  . VAL   A 1 47  ? 19.480 -17.322 11.065  1.00 26.32  ? 226 VAL   A CB  1 
ATOM   355  C  CG1 . VAL   A 1 47  ? 20.126 -18.052 9.898   1.00 26.23  ? 226 VAL   A CG1 1 
ATOM   356  C  CG2 . VAL   A 1 47  ? 19.135 -15.892 10.671  1.00 25.61  ? 226 VAL   A CG2 1 
ATOM   357  N  N   . ARG   A 1 48  ? 19.084 -19.906 12.981  1.00 27.15  ? 227 ARG   A N   1 
ATOM   358  C  CA  . ARG   A 1 48  ? 19.360 -21.296 13.319  1.00 28.48  ? 227 ARG   A CA  1 
ATOM   359  C  C   . ARG   A 1 48  ? 18.057 -22.086 13.416  1.00 28.18  ? 227 ARG   A C   1 
ATOM   360  O  O   . ARG   A 1 48  ? 18.007 -23.241 12.997  1.00 28.14  ? 227 ARG   A O   1 
ATOM   361  C  CB  . ARG   A 1 48  ? 20.210 -21.409 14.590  1.00 30.16  ? 227 ARG   A CB  1 
ATOM   362  C  CG  . ARG   A 1 48  ? 21.695 -21.177 14.353  1.00 32.55  ? 227 ARG   A CG  1 
ATOM   363  C  CD  . ARG   A 1 48  ? 22.580 -21.296 15.582  1.00 34.42  ? 227 ARG   A CD  1 
ATOM   364  N  NE  . ARG   A 1 48  ? 22.306 -20.262 16.573  1.00 35.80  ? 227 ARG   A NE  1 
ATOM   365  C  CZ  . ARG   A 1 48  ? 22.991 -19.130 16.698  1.00 36.64  ? 227 ARG   A CZ  1 
ATOM   366  N  NH1 . ARG   A 1 48  ? 23.960 -18.839 15.845  1.00 36.93  ? 227 ARG   A NH1 1 
ATOM   367  N  NH2 . ARG   A 1 48  ? 22.685 -18.279 17.662  1.00 36.45  ? 227 ARG   A NH2 1 
ATOM   368  N  N   . ALA   A 1 49  ? 17.009 -21.446 13.955  1.00 28.15  ? 228 ALA   A N   1 
ATOM   369  C  CA  . ALA   A 1 49  ? 15.693 -22.056 14.083  1.00 27.83  ? 228 ALA   A CA  1 
ATOM   370  C  C   . ALA   A 1 49  ? 15.132 -22.390 12.703  1.00 27.49  ? 228 ALA   A C   1 
ATOM   371  O  O   . ALA   A 1 49  ? 14.634 -23.494 12.489  1.00 27.36  ? 228 ALA   A O   1 
ATOM   372  C  CB  . ALA   A 1 49  ? 14.763 -21.144 14.849  1.00 28.43  ? 228 ALA   A CB  1 
ATOM   373  N  N   . LEU   A 1 50  ? 15.229 -21.428 11.773  1.00 26.86  ? 229 LEU   A N   1 
ATOM   374  C  CA  . LEU   A 1 50  ? 14.786 -21.623 10.402  1.00 26.37  ? 229 LEU   A CA  1 
ATOM   375  C  C   . LEU   A 1 50  ? 15.523 -22.816 9.797   1.00 26.66  ? 229 LEU   A C   1 
ATOM   376  O  O   . LEU   A 1 50  ? 14.911 -23.646 9.130   1.00 25.87  ? 229 LEU   A O   1 
ATOM   377  C  CB  . LEU   A 1 50  ? 15.038 -20.342 9.597   1.00 26.08  ? 229 LEU   A CB  1 
ATOM   378  C  CG  . LEU   A 1 50  ? 14.144 -19.148 9.936   1.00 26.03  ? 229 LEU   A CG  1 
ATOM   379  C  CD1 . LEU   A 1 50  ? 14.577 -17.912 9.164   1.00 26.02  ? 229 LEU   A CD1 1 
ATOM   380  C  CD2 . LEU   A 1 50  ? 12.681 -19.456 9.651   1.00 25.44  ? 229 LEU   A CD2 1 
ATOM   381  N  N   . HIS   A 1 51  ? 16.835 -22.893 10.057  1.00 27.52  ? 230 HIS   A N   1 
ATOM   382  C  CA  . HIS   A 1 51  ? 17.667 -23.979 9.563   1.00 28.88  ? 230 HIS   A CA  1 
ATOM   383  C  C   . HIS   A 1 51  ? 17.219 -25.303 10.180  1.00 28.75  ? 230 HIS   A C   1 
ATOM   384  O  O   . HIS   A 1 51  ? 17.038 -26.285 9.464   1.00 29.13  ? 230 HIS   A O   1 
ATOM   385  C  CB  . HIS   A 1 51  ? 19.150 -23.698 9.827   1.00 30.48  ? 230 HIS   A CB  1 
ATOM   386  C  CG  . HIS   A 1 51  ? 20.087 -24.647 9.150   1.00 33.21  ? 230 HIS   A CG  1 
ATOM   387  N  ND1 . HIS   A 1 51  ? 21.447 -24.625 9.377   1.00 34.17  ? 230 HIS   A ND1 1 
ATOM   388  C  CD2 . HIS   A 1 51  ? 19.878 -25.631 8.264   1.00 34.05  ? 230 HIS   A CD2 1 
ATOM   389  C  CE1 . HIS   A 1 51  ? 22.029 -25.567 8.648   1.00 35.10  ? 230 HIS   A CE1 1 
ATOM   390  N  NE2 . HIS   A 1 51  ? 21.093 -26.194 7.969   1.00 35.40  ? 230 HIS   A NE2 1 
ATOM   391  N  N   . ASP   A 1 52  ? 17.033 -25.305 11.506  1.00 28.22  ? 231 ASP   A N   1 
ATOM   392  C  CA  . ASP   A 1 52  ? 16.716 -26.509 12.261  1.00 28.88  ? 231 ASP   A CA  1 
ATOM   393  C  C   . ASP   A 1 52  ? 15.343 -27.043 11.860  1.00 28.67  ? 231 ASP   A C   1 
ATOM   394  O  O   . ASP   A 1 52  ? 15.158 -28.255 11.765  1.00 28.79  ? 231 ASP   A O   1 
ATOM   395  C  CB  . ASP   A 1 52  ? 16.795 -26.271 13.773  1.00 29.06  ? 231 ASP   A CB  1 
ATOM   396  C  CG  . ASP   A 1 52  ? 18.206 -26.093 14.314  1.00 30.38  ? 231 ASP   A CG  1 
ATOM   397  O  OD1 . ASP   A 1 52  ? 19.169 -26.361 13.565  1.00 31.25  ? 231 ASP   A OD1 1 
ATOM   398  O  OD2 . ASP   A 1 52  ? 18.333 -25.675 15.481  1.00 31.01  ? 231 ASP   A OD2 1 
ATOM   399  N  N   . THR   A 1 53  ? 14.389 -26.131 11.634  1.00 28.40  ? 232 THR   A N   1 
ATOM   400  C  CA  . THR   A 1 53  ? 13.011 -26.513 11.360  1.00 28.53  ? 232 THR   A CA  1 
ATOM   401  C  C   . THR   A 1 53  ? 12.799 -26.707 9.857   1.00 28.97  ? 232 THR   A C   1 
ATOM   402  O  O   . THR   A 1 53  ? 11.664 -26.856 9.412   1.00 29.49  ? 232 THR   A O   1 
ATOM   403  C  CB  . THR   A 1 53  ? 12.007 -25.551 12.013  1.00 28.35  ? 232 THR   A CB  1 
ATOM   404  O  OG1 . THR   A 1 53  ? 12.173 -24.247 11.456  1.00 29.08  ? 232 THR   A OG1 1 
ATOM   405  C  CG2 . THR   A 1 53  ? 12.134 -25.487 13.521  1.00 28.28  ? 232 THR   A CG2 1 
ATOM   406  N  N   . GLY   A 1 54  ? 13.898 -26.676 9.091   1.00 28.98  ? 233 GLY   A N   1 
ATOM   407  C  CA  . GLY   A 1 54  ? 13.941 -27.129 7.708   1.00 28.24  ? 233 GLY   A CA  1 
ATOM   408  C  C   . GLY   A 1 54  ? 13.175 -26.238 6.732   1.00 27.92  ? 233 GLY   A C   1 
ATOM   409  O  O   . GLY   A 1 54  ? 12.471 -26.743 5.860   1.00 28.00  ? 233 GLY   A O   1 
ATOM   410  N  N   . LYS   A 1 55  ? 13.353 -24.917 6.853   1.00 27.79  ? 234 LYS   A N   1 
ATOM   411  C  CA  . LYS   A 1 55  ? 12.638 -23.965 6.016   1.00 27.78  ? 234 LYS   A CA  1 
ATOM   412  C  C   . LYS   A 1 55  ? 13.467 -23.576 4.792   1.00 28.53  ? 234 LYS   A C   1 
ATOM   413  O  O   . LYS   A 1 55  ? 12.998 -22.808 3.952   1.00 28.28  ? 234 LYS   A O   1 
ATOM   414  C  CB  . LYS   A 1 55  ? 12.231 -22.729 6.828   1.00 27.40  ? 234 LYS   A CB  1 
ATOM   415  C  CG  . LYS   A 1 55  ? 11.276 -22.989 7.986   1.00 26.86  ? 234 LYS   A CG  1 
ATOM   416  C  CD  . LYS   A 1 55  ? 9.961  -23.614 7.559   1.00 26.72  ? 234 LYS   A CD  1 
ATOM   417  C  CE  . LYS   A 1 55  ? 9.096  -24.060 8.721   1.00 26.94  ? 234 LYS   A CE  1 
ATOM   418  N  NZ  . LYS   A 1 55  ? 8.704  -22.926 9.590   1.00 26.94  ? 234 LYS   A NZ  1 
ATOM   419  N  N   . PHE   A 1 56  ? 14.689 -24.115 4.687   1.00 27.85  ? 235 PHE   A N   1 
ATOM   420  C  CA  . PHE   A 1 56  ? 15.605 -23.738 3.620   1.00 27.27  ? 235 PHE   A CA  1 
ATOM   421  C  C   . PHE   A 1 56  ? 15.422 -24.635 2.398   1.00 26.95  ? 235 PHE   A C   1 
ATOM   422  O  O   . PHE   A 1 56  ? 15.144 -25.825 2.524   1.00 26.51  ? 235 PHE   A O   1 
ATOM   423  C  CB  . PHE   A 1 56  ? 17.061 -23.784 4.095   1.00 27.38  ? 235 PHE   A CB  1 
ATOM   424  C  CG  . PHE   A 1 56  ? 17.507 -22.631 4.959   1.00 28.29  ? 235 PHE   A CG  1 
ATOM   425  C  CD1 . PHE   A 1 56  ? 17.067 -22.502 6.268   1.00 28.66  ? 235 PHE   A CD1 1 
ATOM   426  C  CD2 . PHE   A 1 56  ? 18.379 -21.672 4.464   1.00 29.00  ? 235 PHE   A CD2 1 
ATOM   427  C  CE1 . PHE   A 1 56  ? 17.487 -21.442 7.059   1.00 28.88  ? 235 PHE   A CE1 1 
ATOM   428  C  CE2 . PHE   A 1 56  ? 18.795 -20.610 5.253   1.00 29.68  ? 235 PHE   A CE2 1 
ATOM   429  C  CZ  . PHE   A 1 56  ? 18.349 -20.499 6.552   1.00 29.25  ? 235 PHE   A CZ  1 
ATOM   430  N  N   . THR   A 1 57  ? 15.599 -24.033 1.215   1.00 27.86  ? 236 THR   A N   1 
ATOM   431  C  CA  . THR   A 1 57  ? 15.586 -24.729 -0.062  1.00 29.12  ? 236 THR   A CA  1 
ATOM   432  C  C   . THR   A 1 57  ? 17.002 -24.735 -0.633  1.00 30.72  ? 236 THR   A C   1 
ATOM   433  O  O   . THR   A 1 57  ? 17.694 -23.722 -0.579  1.00 29.22  ? 236 THR   A O   1 
ATOM   434  C  CB  . THR   A 1 57  ? 14.639 -24.038 -1.051  1.00 29.43  ? 236 THR   A CB  1 
ATOM   435  O  OG1 . THR   A 1 57  ? 13.364 -23.901 -0.425  1.00 30.39  ? 236 THR   A OG1 1 
ATOM   436  C  CG2 . THR   A 1 57  ? 14.489 -24.786 -2.359  1.00 29.78  ? 236 THR   A CG2 1 
ATOM   437  N  N   . ASP   A 1 58  ? 17.400 -25.876 -1.208  1.00 34.08  ? 237 ASP   A N   1 
ATOM   438  C  CA  . ASP   A 1 58  ? 18.737 -26.066 -1.748  1.00 38.45  ? 237 ASP   A CA  1 
ATOM   439  C  C   . ASP   A 1 58  ? 18.973 -25.087 -2.897  1.00 39.17  ? 237 ASP   A C   1 
ATOM   440  O  O   . ASP   A 1 58  ? 18.099 -24.886 -3.738  1.00 38.43  ? 237 ASP   A O   1 
ATOM   441  C  CB  . ASP   A 1 58  ? 18.964 -27.525 -2.151  1.00 42.66  ? 237 ASP   A CB  1 
ATOM   442  C  CG  . ASP   A 1 58  ? 20.368 -28.019 -1.846  1.00 47.81  ? 237 ASP   A CG  1 
ATOM   443  O  OD1 . ASP   A 1 58  ? 20.749 -28.001 -0.654  1.00 50.16  ? 237 ASP   A OD1 1 
ATOM   444  O  OD2 . ASP   A 1 58  ? 21.067 -28.418 -2.798  1.00 50.97  ? 237 ASP   A OD2 1 
ATOM   445  N  N   . GLY   A 1 59  ? 20.169 -24.485 -2.913  1.00 40.64  ? 238 GLY   A N   1 
ATOM   446  C  CA  . GLY   A 1 59  ? 20.513 -23.407 -3.826  1.00 44.02  ? 238 GLY   A CA  1 
ATOM   447  C  C   . GLY   A 1 59  ? 20.613 -23.858 -5.282  1.00 47.66  ? 238 GLY   A C   1 
ATOM   448  O  O   . GLY   A 1 59  ? 20.223 -23.123 -6.186  1.00 48.08  ? 238 GLY   A O   1 
ATOM   449  N  N   . GLN   A 1 60  ? 21.135 -25.070 -5.503  1.00 50.74  ? 239 GLN   A N   1 
ATOM   450  C  CA  . GLN   A 1 60  ? 21.319 -25.578 -6.854  1.00 54.55  ? 239 GLN   A CA  1 
ATOM   451  C  C   . GLN   A 1 60  ? 19.982 -26.069 -7.410  1.00 55.39  ? 239 GLN   A C   1 
ATOM   452  O  O   . GLN   A 1 60  ? 19.933 -26.758 -8.428  1.00 55.60  ? 239 GLN   A O   1 
ATOM   453  C  CB  . GLN   A 1 60  ? 22.435 -26.626 -6.898  1.00 57.17  ? 239 GLN   A CB  1 
ATOM   454  C  CG  . GLN   A 1 60  ? 22.882 -26.986 -8.311  1.00 60.28  ? 239 GLN   A CG  1 
ATOM   455  C  CD  . GLN   A 1 60  ? 23.383 -25.809 -9.115  1.00 61.68  ? 239 GLN   A CD  1 
ATOM   456  O  OE1 . GLN   A 1 60  ? 23.767 -24.771 -8.578  1.00 63.02  ? 239 GLN   A OE1 1 
ATOM   457  N  NE2 . GLN   A 1 60  ? 23.407 -25.973 -10.428 1.00 62.57  ? 239 GLN   A NE2 1 
ATOM   458  N  N   . LEU   A 1 61  ? 18.898 -25.684 -6.730  1.00 53.84  ? 240 LEU   A N   1 
ATOM   459  C  CA  . LEU   A 1 61  ? 17.550 -25.966 -7.185  1.00 51.32  ? 240 LEU   A CA  1 
ATOM   460  C  C   . LEU   A 1 61  ? 16.906 -24.651 -7.623  1.00 50.94  ? 240 LEU   A C   1 
ATOM   461  O  O   . LEU   A 1 61  ? 16.023 -24.645 -8.479  1.00 51.06  ? 240 LEU   A O   1 
ATOM   462  C  CB  . LEU   A 1 61  ? 16.784 -26.622 -6.032  1.00 50.96  ? 240 LEU   A CB  1 
ATOM   463  C  CG  . LEU   A 1 61  ? 15.848 -27.772 -6.402  1.00 50.75  ? 240 LEU   A CG  1 
ATOM   464  C  CD1 . LEU   A 1 61  ? 15.263 -28.409 -5.152  1.00 49.58  ? 240 LEU   A CD1 1 
ATOM   465  C  CD2 . LEU   A 1 61  ? 14.732 -27.304 -7.321  1.00 52.40  ? 240 LEU   A CD2 1 
ATOM   466  N  N   . VAL   A 1 62  ? 17.379 -23.539 -7.046  1.00 50.76  ? 241 VAL   A N   1 
ATOM   467  C  CA  . VAL   A 1 62  ? 16.829 -22.223 -7.337  1.00 53.12  ? 241 VAL   A CA  1 
ATOM   468  C  C   . VAL   A 1 62  ? 17.469 -21.674 -8.611  1.00 56.08  ? 241 VAL   A C   1 
ATOM   469  O  O   . VAL   A 1 62  ? 16.862 -20.867 -9.312  1.00 55.83  ? 241 VAL   A O   1 
ATOM   470  C  CB  . VAL   A 1 62  ? 16.964 -21.244 -6.150  1.00 52.61  ? 241 VAL   A CB  1 
ATOM   471  C  CG1 . VAL   A 1 62  ? 16.655 -21.909 -4.815  1.00 50.87  ? 241 VAL   A CG1 1 
ATOM   472  C  CG2 . VAL   A 1 62  ? 18.324 -20.567 -6.099  1.00 54.11  ? 241 VAL   A CG2 1 
ATOM   473  N  N   . SER   A 1 63  ? 18.696 -22.125 -8.899  1.00 59.07  ? 242 SER   A N   1 
ATOM   474  C  CA  . SER   A 1 63  ? 19.456 -21.649 -10.043 1.00 62.34  ? 242 SER   A CA  1 
ATOM   475  C  C   . SER   A 1 63  ? 19.762 -22.817 -10.988 1.00 63.48  ? 242 SER   A C   1 
ATOM   476  O  O   . SER   A 1 63  ? 19.157 -22.841 -12.079 1.00 65.22  ? 242 SER   A O   1 
ATOM   477  C  CB  . SER   A 1 63  ? 20.720 -20.954 -9.600  1.00 64.23  ? 242 SER   A CB  1 
ATOM   478  O  OG  . SER   A 1 63  ? 20.427 -19.852 -8.753  1.00 66.16  ? 242 SER   A OG  1 
ATOM   479  N  N   . ASP   A 1 71  ? 27.884 -26.965 -11.545 1.00 71.99  ? 250 ASP   A N   1 
ATOM   480  C  CA  . ASP   A 1 71  ? 26.913 -26.293 -10.639 1.00 71.72  ? 250 ASP   A CA  1 
ATOM   481  C  C   . ASP   A 1 71  ? 27.482 -24.951 -10.175 1.00 71.59  ? 250 ASP   A C   1 
ATOM   482  O  O   . ASP   A 1 71  ? 28.622 -24.611 -10.490 1.00 70.75  ? 250 ASP   A O   1 
ATOM   483  C  CB  . ASP   A 1 71  ? 26.445 -27.229 -9.517  1.00 72.44  ? 250 ASP   A CB  1 
ATOM   484  C  CG  . ASP   A 1 71  ? 27.552 -27.833 -8.668  1.00 72.75  ? 250 ASP   A CG  1 
ATOM   485  O  OD1 . ASP   A 1 71  ? 28.724 -27.445 -8.851  1.00 73.79  ? 250 ASP   A OD1 1 
ATOM   486  O  OD2 . ASP   A 1 71  ? 27.229 -28.699 -7.831  1.00 71.73  ? 250 ASP   A OD2 1 
ATOM   487  N  N   . ILE   A 1 72  ? 26.668 -24.200 -9.424  1.00 70.74  ? 251 ILE   A N   1 
ATOM   488  C  CA  . ILE   A 1 72  ? 26.941 -22.804 -9.115  1.00 69.33  ? 251 ILE   A CA  1 
ATOM   489  C  C   . ILE   A 1 72  ? 27.222 -22.659 -7.620  1.00 66.98  ? 251 ILE   A C   1 
ATOM   490  O  O   . ILE   A 1 72  ? 28.019 -21.813 -7.213  1.00 62.38  ? 251 ILE   A O   1 
ATOM   491  C  CB  . ILE   A 1 72  ? 25.755 -21.917 -9.554  1.00 70.44  ? 251 ILE   A CB  1 
ATOM   492  C  CG1 . ILE   A 1 72  ? 25.238 -22.290 -10.948 1.00 70.91  ? 251 ILE   A CG1 1 
ATOM   493  C  CG2 . ILE   A 1 72  ? 26.107 -20.438 -9.456  1.00 69.73  ? 251 ILE   A CG2 1 
ATOM   494  C  CD1 . ILE   A 1 72  ? 23.917 -21.652 -11.320 1.00 70.37  ? 251 ILE   A CD1 1 
ATOM   495  N  N   . ARG   A 1 73  ? 26.565 -23.503 -6.814  1.00 65.56  ? 252 ARG   A N   1 
ATOM   496  C  CA  . ARG   A 1 73  ? 26.368 -23.211 -5.404  1.00 63.08  ? 252 ARG   A CA  1 
ATOM   497  C  C   . ARG   A 1 73  ? 26.086 -24.491 -4.620  1.00 58.84  ? 252 ARG   A C   1 
ATOM   498  O  O   . ARG   A 1 73  ? 25.527 -25.448 -5.153  1.00 57.14  ? 252 ARG   A O   1 
ATOM   499  C  CB  . ARG   A 1 73  ? 25.213 -22.213 -5.269  1.00 65.11  ? 252 ARG   A CB  1 
ATOM   500  C  CG  . ARG   A 1 73  ? 23.976 -22.588 -6.076  1.00 65.64  ? 252 ARG   A CG  1 
ATOM   501  C  CD  . ARG   A 1 73  ? 23.081 -21.407 -6.395  1.00 66.85  ? 252 ARG   A CD  1 
ATOM   502  N  NE  . ARG   A 1 73  ? 22.354 -20.912 -5.235  1.00 67.78  ? 252 ARG   A NE  1 
ATOM   503  C  CZ  . ARG   A 1 73  ? 21.592 -19.823 -5.225  1.00 70.29  ? 252 ARG   A CZ  1 
ATOM   504  N  NH1 . ARG   A 1 73  ? 21.523 -19.045 -6.291  1.00 72.00  ? 252 ARG   A NH1 1 
ATOM   505  N  NH2 . ARG   A 1 73  ? 20.907 -19.510 -4.140  1.00 72.44  ? 252 ARG   A NH2 1 
ATOM   506  N  N   . GLY   A 1 74  ? 26.491 -24.481 -3.344  1.00 54.53  ? 253 GLY   A N   1 
ATOM   507  C  CA  . GLY   A 1 74  ? 26.156 -25.525 -2.390  1.00 49.66  ? 253 GLY   A CA  1 
ATOM   508  C  C   . GLY   A 1 74  ? 25.389 -24.948 -1.203  1.00 45.91  ? 253 GLY   A C   1 
ATOM   509  O  O   . GLY   A 1 74  ? 25.263 -25.588 -0.162  1.00 44.99  ? 253 GLY   A O   1 
ATOM   510  N  N   . ASP   A 1 75  ? 24.877 -23.727 -1.389  1.00 42.96  ? 254 ASP   A N   1 
ATOM   511  C  CA  . ASP   A 1 75  ? 24.152 -23.005 -0.358  1.00 41.97  ? 254 ASP   A CA  1 
ATOM   512  C  C   . ASP   A 1 75  ? 22.693 -23.455 -0.347  1.00 39.15  ? 254 ASP   A C   1 
ATOM   513  O  O   . ASP   A 1 75  ? 22.266 -24.229 -1.202  1.00 38.53  ? 254 ASP   A O   1 
ATOM   514  C  CB  . ASP   A 1 75  ? 24.221 -21.497 -0.608  1.00 43.90  ? 254 ASP   A CB  1 
ATOM   515  C  CG  . ASP   A 1 75  ? 23.417 -21.062 -1.821  1.00 46.47  ? 254 ASP   A CG  1 
ATOM   516  O  OD1 . ASP   A 1 75  ? 23.677 -21.590 -2.918  1.00 46.60  ? 254 ASP   A OD1 1 
ATOM   517  O  OD2 . ASP   A 1 75  ? 22.530 -20.209 -1.654  1.00 49.42  ? 254 ASP   A OD2 1 
ATOM   518  N  N   . LYS   A 1 76  ? 21.943 -22.951 0.638   1.00 35.75  ? 255 LYS   A N   1 
ATOM   519  C  CA  . LYS   A 1 76  ? 20.499 -23.113 0.691   1.00 33.93  ? 255 LYS   A CA  1 
ATOM   520  C  C   . LYS   A 1 76  ? 19.890 -21.841 1.275   1.00 31.26  ? 255 LYS   A C   1 
ATOM   521  O  O   . LYS   A 1 76  ? 20.515 -21.184 2.107   1.00 30.69  ? 255 LYS   A O   1 
ATOM   522  C  CB  . LYS   A 1 76  ? 20.129 -24.380 1.468   1.00 34.17  ? 255 LYS   A CB  1 
ATOM   523  C  CG  . LYS   A 1 76  ? 20.598 -24.424 2.914   1.00 34.96  ? 255 LYS   A CG  1 
ATOM   524  C  CD  . LYS   A 1 76  ? 20.401 -25.780 3.545   1.00 36.28  ? 255 LYS   A CD  1 
ATOM   525  C  CE  . LYS   A 1 76  ? 20.755 -25.797 5.015   1.00 37.09  ? 255 LYS   A CE  1 
ATOM   526  N  NZ  . LYS   A 1 76  ? 22.174 -25.443 5.247   1.00 37.63  ? 255 LYS   A NZ  1 
ATOM   527  N  N   . ILE   A 1 77  ? 18.679 -21.496 0.819   1.00 29.17  ? 256 ILE   A N   1 
ATOM   528  C  CA  . ILE   A 1 77  ? 18.103 -20.188 1.104   1.00 28.33  ? 256 ILE   A CA  1 
ATOM   529  C  C   . ILE   A 1 77  ? 16.661 -20.311 1.594   1.00 28.35  ? 256 ILE   A C   1 
ATOM   530  O  O   . ILE   A 1 77  ? 16.007 -21.337 1.405   1.00 26.00  ? 256 ILE   A O   1 
ATOM   531  C  CB  . ILE   A 1 77  ? 18.194 -19.247 -0.116  1.00 28.30  ? 256 ILE   A CB  1 
ATOM   532  C  CG1 . ILE   A 1 77  ? 17.422 -19.794 -1.322  1.00 28.64  ? 256 ILE   A CG1 1 
ATOM   533  C  CG2 . ILE   A 1 77  ? 19.644 -18.920 -0.454  1.00 28.01  ? 256 ILE   A CG2 1 
ATOM   534  C  CD1 . ILE   A 1 77  ? 17.103 -18.757 -2.374  1.00 29.35  ? 256 ILE   A CD1 1 
ATOM   535  N  N   . THR   A 1 78  ? 16.188 -19.221 2.212   1.00 28.54  ? 257 THR   A N   1 
ATOM   536  C  CA  . THR   A 1 78  ? 14.786 -19.020 2.547   1.00 29.70  ? 257 THR   A CA  1 
ATOM   537  C  C   . THR   A 1 78  ? 14.482 -17.520 2.523   1.00 29.79  ? 257 THR   A C   1 
ATOM   538  O  O   . THR   A 1 78  ? 15.302 -16.713 2.961   1.00 29.08  ? 257 THR   A O   1 
ATOM   539  C  CB  . THR   A 1 78  ? 14.419 -19.714 3.868   1.00 30.53  ? 257 THR   A CB  1 
ATOM   540  O  OG1 . THR   A 1 78  ? 13.011 -19.587 4.058   1.00 33.32  ? 257 THR   A OG1 1 
ATOM   541  C  CG2 . THR   A 1 78  ? 15.143 -19.157 5.076   1.00 30.42  ? 257 THR   A CG2 1 
ATOM   542  N  N   . TRP   A 1 79  ? 13.303 -17.168 1.991   1.00 28.57  ? 258 TRP   A N   1 
ATOM   543  C  CA  . TRP   A 1 79  ? 12.843 -15.791 1.887   1.00 27.94  ? 258 TRP   A CA  1 
ATOM   544  C  C   . TRP   A 1 79  ? 12.025 -15.418 3.121   1.00 27.94  ? 258 TRP   A C   1 
ATOM   545  O  O   . TRP   A 1 79  ? 11.103 -16.138 3.501   1.00 28.23  ? 258 TRP   A O   1 
ATOM   546  C  CB  . TRP   A 1 79  ? 12.031 -15.589 0.600   1.00 28.23  ? 258 TRP   A CB  1 
ATOM   547  C  CG  . TRP   A 1 79  ? 12.846 -15.604 -0.657  1.00 27.99  ? 258 TRP   A CG  1 
ATOM   548  C  CD1 . TRP   A 1 79  ? 12.926 -16.615 -1.570  1.00 29.32  ? 258 TRP   A CD1 1 
ATOM   549  C  CD2 . TRP   A 1 79  ? 13.675 -14.542 -1.164  1.00 28.19  ? 258 TRP   A CD2 1 
ATOM   550  N  NE1 . TRP   A 1 79  ? 13.760 -16.266 -2.600  1.00 29.43  ? 258 TRP   A NE1 1 
ATOM   551  C  CE2 . TRP   A 1 79  ? 14.234 -14.999 -2.378  1.00 29.75  ? 258 TRP   A CE2 1 
ATOM   552  C  CE3 . TRP   A 1 79  ? 14.008 -13.259 -0.711  1.00 28.29  ? 258 TRP   A CE3 1 
ATOM   553  C  CZ2 . TRP   A 1 79  ? 15.106 -14.217 -3.139  1.00 29.35  ? 258 TRP   A CZ2 1 
ATOM   554  C  CZ3 . TRP   A 1 79  ? 14.865 -12.486 -1.465  1.00 28.40  ? 258 TRP   A CZ3 1 
ATOM   555  C  CH2 . TRP   A 1 79  ? 15.407 -12.961 -2.662  1.00 28.82  ? 258 TRP   A CH2 1 
ATOM   556  N  N   . ILE   A 1 80  ? 12.366 -14.277 3.732   1.00 27.55  ? 259 ILE   A N   1 
ATOM   557  C  CA  . ILE   A 1 80  ? 11.707 -13.820 4.948   1.00 28.71  ? 259 ILE   A CA  1 
ATOM   558  C  C   . ILE   A 1 80  ? 11.136 -12.422 4.715   1.00 29.97  ? 259 ILE   A C   1 
ATOM   559  O  O   . ILE   A 1 80  ? 11.860 -11.513 4.313   1.00 30.06  ? 259 ILE   A O   1 
ATOM   560  C  CB  . ILE   A 1 80  ? 12.672 -13.872 6.154   1.00 28.08  ? 259 ILE   A CB  1 
ATOM   561  C  CG1 . ILE   A 1 80  ? 13.164 -15.295 6.443   1.00 28.97  ? 259 ILE   A CG1 1 
ATOM   562  C  CG2 . ILE   A 1 80  ? 12.061 -13.217 7.389   1.00 28.38  ? 259 ILE   A CG2 1 
ATOM   563  C  CD1 . ILE   A 1 80  ? 12.070 -16.305 6.746   1.00 28.90  ? 259 ILE   A CD1 1 
ATOM   564  N  N   . GLU   A 1 81  ? 9.831  -12.275 4.984   1.00 30.30  ? 260 GLU   A N   1 
ATOM   565  C  CA  . GLU   A 1 81  ? 9.113  -11.020 4.816   1.00 31.54  ? 260 GLU   A CA  1 
ATOM   566  C  C   . GLU   A 1 81  ? 9.400  -10.107 6.007   1.00 30.73  ? 260 GLU   A C   1 
ATOM   567  O  O   . GLU   A 1 81  ? 9.489  -8.892  5.850   1.00 30.26  ? 260 GLU   A O   1 
ATOM   568  C  CB  . GLU   A 1 81  ? 7.614  -11.288 4.630   1.00 33.92  ? 260 GLU   A CB  1 
ATOM   569  C  CG  . GLU   A 1 81  ? 6.807  -10.070 4.202   1.00 36.22  ? 260 GLU   A CG  1 
ATOM   570  C  CD  . GLU   A 1 81  ? 6.401  -9.104  5.304   1.00 37.89  ? 260 GLU   A CD  1 
ATOM   571  O  OE1 . GLU   A 1 81  ? 6.480  -9.488  6.489   1.00 38.00  ? 260 GLU   A OE1 1 
ATOM   572  O  OE2 . GLU   A 1 81  ? 6.023  -7.959  4.975   1.00 38.74  ? 260 GLU   A OE2 1 
ATOM   573  N  N   . GLY   A 1 82  ? 9.521  -10.704 7.199   1.00 30.86  ? 261 GLY   A N   1 
ATOM   574  C  CA  . GLY   A 1 82  ? 9.933  -9.973  8.386   1.00 30.94  ? 261 GLY   A CA  1 
ATOM   575  C  C   . GLY   A 1 82  ? 8.906  -10.019 9.518   1.00 31.71  ? 261 GLY   A C   1 
ATOM   576  O  O   . GLY   A 1 82  ? 9.245  -9.727  10.663  1.00 31.38  ? 261 GLY   A O   1 
ATOM   577  N  N   . LYS   A 1 83  ? 7.661  -10.390 9.197   1.00 33.74  ? 262 LYS   A N   1 
ATOM   578  C  CA  . LYS   A 1 83  ? 6.581  -10.350 10.174  1.00 35.89  ? 262 LYS   A CA  1 
ATOM   579  C  C   . LYS   A 1 83  ? 6.190  -11.760 10.618  1.00 35.74  ? 262 LYS   A C   1 
ATOM   580  O  O   . LYS   A 1 83  ? 5.301  -11.914 11.456  1.00 35.35  ? 262 LYS   A O   1 
ATOM   581  C  CB  . LYS   A 1 83  ? 5.358  -9.611  9.621   1.00 38.48  ? 262 LYS   A CB  1 
ATOM   582  C  CG  . LYS   A 1 83  ? 5.582  -8.161  9.216   1.00 41.23  ? 262 LYS   A CG  1 
ATOM   583  C  CD  . LYS   A 1 83  ? 4.330  -7.504  8.672   1.00 43.43  ? 262 LYS   A CD  1 
ATOM   584  C  CE  . LYS   A 1 83  ? 4.612  -6.274  7.835   1.00 46.60  ? 262 LYS   A CE  1 
ATOM   585  N  NZ  . LYS   A 1 83  ? 5.416  -5.266  8.569   1.00 48.70  ? 262 LYS   A NZ  1 
ATOM   586  N  N   . GLU   A 1 84  ? 6.857  -12.780 10.060  1.00 34.16  ? 263 GLU   A N   1 
ATOM   587  C  CA  . GLU   A 1 84  ? 6.563  -14.164 10.401  1.00 32.85  ? 263 GLU   A CA  1 
ATOM   588  C  C   . GLU   A 1 84  ? 6.852  -14.398 11.881  1.00 32.65  ? 263 GLU   A C   1 
ATOM   589  O  O   . GLU   A 1 84  ? 7.784  -13.810 12.431  1.00 33.59  ? 263 GLU   A O   1 
ATOM   590  C  CB  . GLU   A 1 84  ? 7.395  -15.150 9.578   1.00 32.05  ? 263 GLU   A CB  1 
ATOM   591  C  CG  . GLU   A 1 84  ? 7.203  -15.043 8.077   1.00 31.51  ? 263 GLU   A CG  1 
ATOM   592  C  CD  . GLU   A 1 84  ? 8.100  -14.032 7.382   1.00 31.26  ? 263 GLU   A CD  1 
ATOM   593  O  OE1 . GLU   A 1 84  ? 8.700  -13.184 8.080   1.00 30.35  ? 263 GLU   A OE1 1 
ATOM   594  O  OE2 . GLU   A 1 84  ? 8.215  -14.112 6.144   1.00 31.31  ? 263 GLU   A OE2 1 
ATOM   595  N  N   . PRO   A 1 85  ? 6.062  -15.258 12.569  1.00 32.43  ? 264 PRO   A N   1 
ATOM   596  C  CA  . PRO   A 1 85  ? 6.373  -15.662 13.942  1.00 31.46  ? 264 PRO   A CA  1 
ATOM   597  C  C   . PRO   A 1 85  ? 7.774  -16.264 14.001  1.00 31.01  ? 264 PRO   A C   1 
ATOM   598  O  O   . PRO   A 1 85  ? 8.109  -17.140 13.204  1.00 31.45  ? 264 PRO   A O   1 
ATOM   599  C  CB  . PRO   A 1 85  ? 5.327  -16.749 14.241  1.00 31.88  ? 264 PRO   A CB  1 
ATOM   600  C  CG  . PRO   A 1 85  ? 4.172  -16.414 13.323  1.00 32.30  ? 264 PRO   A CG  1 
ATOM   601  C  CD  . PRO   A 1 85  ? 4.824  -15.877 12.065  1.00 31.77  ? 264 PRO   A CD  1 
ATOM   602  N  N   . GLY   A 1 86  ? 8.594  -15.756 14.926  1.00 30.32  ? 265 GLY   A N   1 
ATOM   603  C  CA  . GLY   A 1 86  ? 9.943  -16.259 15.130  1.00 31.10  ? 265 GLY   A CA  1 
ATOM   604  C  C   . GLY   A 1 86  ? 10.983 -15.543 14.269  1.00 31.42  ? 265 GLY   A C   1 
ATOM   605  O  O   . GLY   A 1 86  ? 12.156 -15.909 14.296  1.00 31.58  ? 265 GLY   A O   1 
ATOM   606  N  N   . CYS   A 1 87  ? 10.548 -14.520 13.520  1.00 31.56  ? 266 CYS   A N   1 
ATOM   607  C  CA  . CYS   A 1 87  ? 11.406 -13.813 12.577  1.00 30.90  ? 266 CYS   A CA  1 
ATOM   608  C  C   . CYS   A 1 87  ? 11.377 -12.309 12.849  1.00 31.42  ? 266 CYS   A C   1 
ATOM   609  O  O   . CYS   A 1 87  ? 11.773 -11.517 11.995  1.00 31.16  ? 266 CYS   A O   1 
ATOM   610  C  CB  . CYS   A 1 87  ? 10.951 -14.055 11.141  1.00 30.58  ? 266 CYS   A CB  1 
ATOM   611  S  SG  . CYS   A 1 87  ? 11.100 -15.775 10.593  1.00 31.26  ? 266 CYS   A SG  1 
ATOM   612  N  N   . GLU   A 1 88  ? 10.926 -11.931 14.052  1.00 31.82  ? 267 GLU   A N   1 
ATOM   613  C  CA  . GLU   A 1 88  ? 10.698 -10.539 14.416  1.00 32.53  ? 267 GLU   A CA  1 
ATOM   614  C  C   . GLU   A 1 88  ? 12.003 -9.742  14.386  1.00 30.72  ? 267 GLU   A C   1 
ATOM   615  O  O   . GLU   A 1 88  ? 12.002 -8.569  14.021  1.00 29.71  ? 267 GLU   A O   1 
ATOM   616  C  CB  . GLU   A 1 88  ? 10.018 -10.426 15.785  1.00 34.92  ? 267 GLU   A CB  1 
ATOM   617  C  CG  . GLU   A 1 88  ? 8.628  -11.044 15.825  1.00 38.34  ? 267 GLU   A CG  1 
ATOM   618  C  CD  . GLU   A 1 88  ? 8.551  -12.524 16.170  1.00 40.63  ? 267 GLU   A CD  1 
ATOM   619  O  OE1 . GLU   A 1 88  ? 9.503  -13.262 15.846  1.00 41.26  ? 267 GLU   A OE1 1 
ATOM   620  O  OE2 . GLU   A 1 88  ? 7.518  -12.945 16.735  1.00 42.02  ? 267 GLU   A OE2 1 
ATOM   621  N  N   . THR   A 1 89  ? 13.110 -10.379 14.783  1.00 29.82  ? 268 THR   A N   1 
ATOM   622  C  CA  . THR   A 1 89  ? 14.386 -9.684  14.867  1.00 28.96  ? 268 THR   A CA  1 
ATOM   623  C  C   . THR   A 1 89  ? 14.961 -9.486  13.464  1.00 27.97  ? 268 THR   A C   1 
ATOM   624  O  O   . THR   A 1 89  ? 15.594 -8.467  13.192  1.00 26.42  ? 268 THR   A O   1 
ATOM   625  C  CB  . THR   A 1 89  ? 15.341 -10.365 15.857  1.00 29.60  ? 268 THR   A CB  1 
ATOM   626  O  OG1 . THR   A 1 89  ? 14.573 -10.838 16.964  1.00 30.47  ? 268 THR   A OG1 1 
ATOM   627  C  CG2 . THR   A 1 89  ? 16.429 -9.441  16.358  1.00 30.25  ? 268 THR   A CG2 1 
ATOM   628  N  N   . ILE   A 1 90  ? 14.724 -10.461 12.575  1.00 27.07  ? 269 ILE   A N   1 
ATOM   629  C  CA  . ILE   A 1 90  ? 15.066 -10.305 11.169  1.00 27.07  ? 269 ILE   A CA  1 
ATOM   630  C  C   . ILE   A 1 90  ? 14.275 -9.123  10.611  1.00 27.54  ? 269 ILE   A C   1 
ATOM   631  O  O   . ILE   A 1 90  ? 14.810 -8.325  9.844   1.00 27.31  ? 269 ILE   A O   1 
ATOM   632  C  CB  . ILE   A 1 90  ? 14.834 -11.612 10.381  1.00 26.92  ? 269 ILE   A CB  1 
ATOM   633  C  CG1 . ILE   A 1 90  ? 15.705 -12.750 10.923  1.00 26.62  ? 269 ILE   A CG1 1 
ATOM   634  C  CG2 . ILE   A 1 90  ? 15.063 -11.392 8.889   1.00 26.50  ? 269 ILE   A CG2 1 
ATOM   635  C  CD1 . ILE   A 1 90  ? 15.286 -14.131 10.466  1.00 26.37  ? 269 ILE   A CD1 1 
ATOM   636  N  N   . GLY   A 1 91  ? 13.015 -9.001  11.050  1.00 27.80  ? 270 GLY   A N   1 
ATOM   637  C  CA  . GLY   A 1 91  ? 12.156 -7.881  10.694  1.00 27.85  ? 270 GLY   A CA  1 
ATOM   638  C  C   . GLY   A 1 91  ? 12.765 -6.531  11.071  1.00 28.04  ? 270 GLY   A C   1 
ATOM   639  O  O   . GLY   A 1 91  ? 12.714 -5.589  10.281  1.00 28.63  ? 270 GLY   A O   1 
ATOM   640  N  N   . LEU   A 1 92  ? 13.339 -6.451  12.280  1.00 27.83  ? 271 LEU   A N   1 
ATOM   641  C  CA  . LEU   A 1 92  ? 13.960 -5.229  12.773  1.00 28.50  ? 271 LEU   A CA  1 
ATOM   642  C  C   . LEU   A 1 92  ? 15.228 -4.914  11.978  1.00 27.67  ? 271 LEU   A C   1 
ATOM   643  O  O   . LEU   A 1 92  ? 15.485 -3.753  11.661  1.00 28.35  ? 271 LEU   A O   1 
ATOM   644  C  CB  . LEU   A 1 92  ? 14.248 -5.359  14.275  1.00 29.65  ? 271 LEU   A CB  1 
ATOM   645  C  CG  . LEU   A 1 92  ? 15.153 -4.285  14.883  1.00 31.53  ? 271 LEU   A CG  1 
ATOM   646  C  CD1 . LEU   A 1 92  ? 14.488 -2.914  14.857  1.00 32.47  ? 271 LEU   A CD1 1 
ATOM   647  C  CD2 . LEU   A 1 92  ? 15.550 -4.650  16.306  1.00 32.06  ? 271 LEU   A CD2 1 
ATOM   648  N  N   . LEU   A 1 93  ? 16.021 -5.949  11.668  1.00 26.72  ? 272 LEU   A N   1 
ATOM   649  C  CA  . LEU   A 1 93  ? 17.201 -5.772  10.834  1.00 26.04  ? 272 LEU   A CA  1 
ATOM   650  C  C   . LEU   A 1 93  ? 16.791 -5.123  9.513   1.00 26.18  ? 272 LEU   A C   1 
ATOM   651  O  O   . LEU   A 1 93  ? 17.430 -4.181  9.049   1.00 27.13  ? 272 LEU   A O   1 
ATOM   652  C  CB  . LEU   A 1 93  ? 17.878 -7.128  10.596  1.00 25.16  ? 272 LEU   A CB  1 
ATOM   653  C  CG  . LEU   A 1 93  ? 18.870 -7.177  9.430   1.00 24.77  ? 272 LEU   A CG  1 
ATOM   654  C  CD1 . LEU   A 1 93  ? 20.143 -6.400  9.748   1.00 24.27  ? 272 LEU   A CD1 1 
ATOM   655  C  CD2 . LEU   A 1 93  ? 19.202 -8.612  9.044   1.00 24.17  ? 272 LEU   A CD2 1 
ATOM   656  N  N   . MET   A 1 94  ? 15.713 -5.646  8.924   1.00 26.57  ? 273 MET   A N   1 
ATOM   657  C  CA  . MET   A 1 94  ? 15.248 -5.223  7.614   1.00 26.67  ? 273 MET   A CA  1 
ATOM   658  C  C   . MET   A 1 94  ? 14.779 -3.769  7.674   1.00 26.09  ? 273 MET   A C   1 
ATOM   659  O  O   . MET   A 1 94  ? 15.052 -2.992  6.762   1.00 24.91  ? 273 MET   A O   1 
ATOM   660  C  CB  . MET   A 1 94  ? 14.114 -6.135  7.138   1.00 27.29  ? 273 MET   A CB  1 
ATOM   661  C  CG  . MET   A 1 94  ? 14.609 -7.495  6.664   1.00 27.74  ? 273 MET   A CG  1 
ATOM   662  S  SD  . MET   A 1 94  ? 13.270 -8.709  6.515   1.00 29.02  ? 273 MET   A SD  1 
ATOM   663  C  CE  . MET   A 1 94  ? 12.604 -8.225  4.923   1.00 28.71  ? 273 MET   A CE  1 
ATOM   664  N  N   . SER   A 1 95  ? 14.110 -3.393  8.772   1.00 26.12  ? 274 SER   A N   1 
ATOM   665  C  CA  . SER   A 1 95  ? 13.654 -2.020  8.927   1.00 27.13  ? 274 SER   A CA  1 
ATOM   666  C  C   . SER   A 1 95  ? 14.834 -1.079  9.169   1.00 26.86  ? 274 SER   A C   1 
ATOM   667  O  O   . SER   A 1 95  ? 14.782 0.079   8.766   1.00 27.27  ? 274 SER   A O   1 
ATOM   668  C  CB  . SER   A 1 95  ? 12.585 -1.884  9.991   1.00 29.12  ? 274 SER   A CB  1 
ATOM   669  O  OG  . SER   A 1 95  ? 13.125 -2.092  11.287  1.00 31.72  ? 274 SER   A OG  1 
ATOM   670  N  N   . SER   A 1 96  ? 15.896 -1.589  9.810   1.00 26.49  ? 275 SER   A N   1 
ATOM   671  C  CA  . SER   A 1 96  ? 17.094 -0.809  10.087  1.00 26.73  ? 275 SER   A CA  1 
ATOM   672  C  C   . SER   A 1 96  ? 17.856 -0.542  8.790   1.00 26.54  ? 275 SER   A C   1 
ATOM   673  O  O   . SER   A 1 96  ? 18.381 0.550   8.582   1.00 25.74  ? 275 SER   A O   1 
ATOM   674  C  CB  . SER   A 1 96  ? 17.968 -1.498  11.108  1.00 27.12  ? 275 SER   A CB  1 
ATOM   675  O  OG  . SER   A 1 96  ? 17.236 -1.775  12.293  1.00 27.74  ? 275 SER   A OG  1 
ATOM   676  N  N   . MET   A 1 97  ? 17.906 -1.561  7.924   1.00 26.44  ? 276 MET   A N   1 
ATOM   677  C  CA  . MET   A 1 97  ? 18.479 -1.437  6.593   1.00 26.84  ? 276 MET   A CA  1 
ATOM   678  C  C   . MET   A 1 97  ? 17.729 -0.355  5.817   1.00 26.88  ? 276 MET   A C   1 
ATOM   679  O  O   . MET   A 1 97  ? 18.349 0.495   5.180   1.00 27.63  ? 276 MET   A O   1 
ATOM   680  C  CB  . MET   A 1 97  ? 18.345 -2.761  5.838   1.00 26.88  ? 276 MET   A CB  1 
ATOM   681  C  CG  . MET   A 1 97  ? 19.354 -3.813  6.242   1.00 27.59  ? 276 MET   A CG  1 
ATOM   682  S  SD  . MET   A 1 97  ? 19.008 -5.313  5.298   1.00 30.01  ? 276 MET   A SD  1 
ATOM   683  C  CE  . MET   A 1 97  ? 20.225 -6.432  5.990   1.00 29.58  ? 276 MET   A CE  1 
ATOM   684  N  N   . ASP   A 1 98  ? 16.392 -0.407  5.879   1.00 27.00  ? 277 ASP   A N   1 
ATOM   685  C  CA  . ASP   A 1 98  ? 15.513 0.529   5.190   1.00 27.88  ? 277 ASP   A CA  1 
ATOM   686  C  C   . ASP   A 1 98  ? 15.805 1.965   5.626   1.00 28.48  ? 277 ASP   A C   1 
ATOM   687  O  O   . ASP   A 1 98  ? 15.862 2.864   4.788   1.00 28.33  ? 277 ASP   A O   1 
ATOM   688  C  CB  . ASP   A 1 98  ? 14.040 0.161   5.398   1.00 28.04  ? 277 ASP   A CB  1 
ATOM   689  C  CG  . ASP   A 1 98  ? 13.620 -1.119  4.693   1.00 28.77  ? 277 ASP   A CG  1 
ATOM   690  O  OD1 . ASP   A 1 98  ? 14.408 -1.624  3.864   1.00 29.23  ? 277 ASP   A OD1 1 
ATOM   691  O  OD2 . ASP   A 1 98  ? 12.513 -1.614  4.989   1.00 29.75  ? 277 ASP   A OD2 1 
ATOM   692  N  N   . ASP   A 1 99  ? 15.984 2.161   6.939   1.00 29.58  ? 278 ASP   A N   1 
ATOM   693  C  CA  . ASP   A 1 99  ? 16.235 3.469   7.530   1.00 30.78  ? 278 ASP   A CA  1 
ATOM   694  C  C   . ASP   A 1 99  ? 17.494 4.094   6.931   1.00 30.12  ? 278 ASP   A C   1 
ATOM   695  O  O   . ASP   A 1 99  ? 17.478 5.265   6.553   1.00 29.88  ? 278 ASP   A O   1 
ATOM   696  C  CB  . ASP   A 1 99  ? 16.333 3.389   9.056   1.00 32.75  ? 278 ASP   A CB  1 
ATOM   697  C  CG  . ASP   A 1 99  ? 15.017 3.078   9.751   1.00 35.88  ? 278 ASP   A CG  1 
ATOM   698  O  OD1 . ASP   A 1 99  ? 13.972 3.059   9.066   1.00 37.93  ? 278 ASP   A OD1 1 
ATOM   699  O  OD2 . ASP   A 1 99  ? 15.049 2.844   10.975  1.00 37.88  ? 278 ASP   A OD2 1 
ATOM   700  N  N   . LEU   A 1 100 ? 18.576 3.306   6.855   1.00 27.74  ? 279 LEU   A N   1 
ATOM   701  C  CA  . LEU   A 1 100 ? 19.830 3.756   6.267   1.00 28.06  ? 279 LEU   A CA  1 
ATOM   702  C  C   . LEU   A 1 100 ? 19.605 4.207   4.826   1.00 28.14  ? 279 LEU   A C   1 
ATOM   703  O  O   . LEU   A 1 100 ? 20.028 5.298   4.441   1.00 29.01  ? 279 LEU   A O   1 
ATOM   704  C  CB  . LEU   A 1 100 ? 20.865 2.625   6.326   1.00 27.83  ? 279 LEU   A CB  1 
ATOM   705  C  CG  . LEU   A 1 100 ? 21.484 2.343   7.694   1.00 27.15  ? 279 LEU   A CG  1 
ATOM   706  C  CD1 . LEU   A 1 100 ? 22.627 1.352   7.565   1.00 26.17  ? 279 LEU   A CD1 1 
ATOM   707  C  CD2 . LEU   A 1 100 ? 21.980 3.624   8.352   1.00 27.06  ? 279 LEU   A CD2 1 
ATOM   708  N  N   . ILE   A 1 101 ? 18.939 3.352   4.040   1.00 28.12  ? 280 ILE   A N   1 
ATOM   709  C  CA  . ILE   A 1 101 ? 18.710 3.598   2.623   1.00 28.63  ? 280 ILE   A CA  1 
ATOM   710  C  C   . ILE   A 1 101 ? 17.871 4.864   2.438   1.00 29.26  ? 280 ILE   A C   1 
ATOM   711  O  O   . ILE   A 1 101 ? 18.171 5.676   1.565   1.00 30.03  ? 280 ILE   A O   1 
ATOM   712  C  CB  . ILE   A 1 101 ? 18.092 2.360   1.941   1.00 28.63  ? 280 ILE   A CB  1 
ATOM   713  C  CG1 . ILE   A 1 101 ? 19.112 1.225   1.794   1.00 28.11  ? 280 ILE   A CG1 1 
ATOM   714  C  CG2 . ILE   A 1 101 ? 17.453 2.715   0.605   1.00 28.26  ? 280 ILE   A CG2 1 
ATOM   715  C  CD1 . ILE   A 1 101 ? 20.304 1.547   0.912   1.00 28.29  ? 280 ILE   A CD1 1 
ATOM   716  N  N   . ARG   A 1 102 ? 16.832 5.028   3.268   1.00 29.96  ? 281 ARG   A N   1 
ATOM   717  C  CA  . ARG   A 1 102 ? 15.972 6.202   3.213   1.00 31.57  ? 281 ARG   A CA  1 
ATOM   718  C  C   . ARG   A 1 102 ? 16.800 7.481   3.331   1.00 31.52  ? 281 ARG   A C   1 
ATOM   719  O  O   . ARG   A 1 102 ? 16.534 8.453   2.628   1.00 30.76  ? 281 ARG   A O   1 
ATOM   720  C  CB  . ARG   A 1 102 ? 14.873 6.151   4.281   1.00 33.96  ? 281 ARG   A CB  1 
ATOM   721  C  CG  . ARG   A 1 102 ? 13.612 5.415   3.850   1.00 37.97  ? 281 ARG   A CG  1 
ATOM   722  C  CD  . ARG   A 1 102 ? 12.441 5.653   4.789   1.00 41.13  ? 281 ARG   A CD  1 
ATOM   723  N  NE  . ARG   A 1 102 ? 12.442 4.803   5.974   1.00 44.40  ? 281 ARG   A NE  1 
ATOM   724  C  CZ  . ARG   A 1 102 ? 12.033 3.536   6.000   1.00 47.37  ? 281 ARG   A CZ  1 
ATOM   725  N  NH1 . ARG   A 1 102 ? 11.495 2.986   4.925   1.00 48.40  ? 281 ARG   A NH1 1 
ATOM   726  N  NH2 . ARG   A 1 102 ? 12.144 2.827   7.111   1.00 48.08  ? 281 ARG   A NH2 1 
ATOM   727  N  N   . HIS   A 1 103 ? 17.805 7.470   4.217   1.00 31.82  ? 282 HIS   A N   1 
ATOM   728  C  CA  . HIS   A 1 103 ? 18.636 8.640   4.459   1.00 33.05  ? 282 HIS   A CA  1 
ATOM   729  C  C   . HIS   A 1 103 ? 19.675 8.819   3.353   1.00 34.01  ? 282 HIS   A C   1 
ATOM   730  O  O   . HIS   A 1 103 ? 20.274 9.888   3.249   1.00 35.45  ? 282 HIS   A O   1 
ATOM   731  C  CB  . HIS   A 1 103 ? 19.250 8.601   5.863   1.00 32.76  ? 282 HIS   A CB  1 
ATOM   732  C  CG  . HIS   A 1 103 ? 18.258 8.793   6.962   1.00 33.72  ? 282 HIS   A CG  1 
ATOM   733  N  ND1 . HIS   A 1 103 ? 17.469 9.918   7.067   1.00 33.83  ? 282 HIS   A ND1 1 
ATOM   734  C  CD2 . HIS   A 1 103 ? 17.930 8.013   8.001   1.00 33.48  ? 282 HIS   A CD2 1 
ATOM   735  C  CE1 . HIS   A 1 103 ? 16.691 9.808   8.136   1.00 33.49  ? 282 HIS   A CE1 1 
ATOM   736  N  NE2 . HIS   A 1 103 ? 16.957 8.659   8.719   1.00 33.51  ? 282 HIS   A NE2 1 
ATOM   737  N  N   . CYS   A 1 104 ? 19.879 7.778   2.533   1.00 34.76  ? 283 CYS   A N   1 
ATOM   738  C  CA  . CYS   A 1 104 ? 20.787 7.841   1.396   1.00 36.67  ? 283 CYS   A CA  1 
ATOM   739  C  C   . CYS   A 1 104 ? 20.062 8.353   0.155   1.00 39.34  ? 283 CYS   A C   1 
ATOM   740  O  O   . CYS   A 1 104 ? 20.619 9.143   -0.604  1.00 41.12  ? 283 CYS   A O   1 
ATOM   741  C  CB  . CYS   A 1 104 ? 21.330 6.465   1.033   1.00 35.19  ? 283 CYS   A CB  1 
ATOM   742  S  SG  . CYS   A 1 104 ? 22.510 5.801   2.232   1.00 34.26  ? 283 CYS   A SG  1 
ATOM   743  N  N   . ASN   A 1 105 ? 18.828 7.870   -0.042  1.00 41.17  ? 284 ASN   A N   1 
ATOM   744  C  CA  . ASN   A 1 105 ? 18.102 7.992   -1.298  1.00 42.13  ? 284 ASN   A CA  1 
ATOM   745  C  C   . ASN   A 1 105 ? 18.271 9.388   -1.897  1.00 40.94  ? 284 ASN   A C   1 
ATOM   746  O  O   . ASN   A 1 105 ? 18.113 10.398  -1.211  1.00 39.69  ? 284 ASN   A O   1 
ATOM   747  C  CB  . ASN   A 1 105 ? 16.632 7.589   -1.152  1.00 45.12  ? 284 ASN   A CB  1 
ATOM   748  C  CG  . ASN   A 1 105 ? 15.894 7.582   -2.474  1.00 46.90  ? 284 ASN   A CG  1 
ATOM   749  O  OD1 . ASN   A 1 105 ? 16.313 6.920   -3.421  1.00 47.76  ? 284 ASN   A OD1 1 
ATOM   750  N  ND2 . ASN   A 1 105 ? 14.806 8.330   -2.551  1.00 47.13  ? 284 ASN   A ND2 1 
ATOM   751  N  N   . GLY   A 1 106 ? 18.598 9.414   -3.193  1.00 40.01  ? 285 GLY   A N   1 
ATOM   752  C  CA  . GLY   A 1 106 ? 18.836 10.646  -3.925  1.00 39.47  ? 285 GLY   A CA  1 
ATOM   753  C  C   . GLY   A 1 106 ? 20.319 11.001  -3.993  1.00 39.53  ? 285 GLY   A C   1 
ATOM   754  O  O   . GLY   A 1 106 ? 20.699 11.932  -4.701  1.00 41.22  ? 285 GLY   A O   1 
ATOM   755  N  N   . LYS   A 1 107 ? 21.148 10.255  -3.254  1.00 37.57  ? 286 LYS   A N   1 
ATOM   756  C  CA  . LYS   A 1 107 ? 22.571 10.552  -3.175  1.00 37.93  ? 286 LYS   A CA  1 
ATOM   757  C  C   . LYS   A 1 107 ? 23.401 9.339   -3.596  1.00 37.61  ? 286 LYS   A C   1 
ATOM   758  O  O   . LYS   A 1 107 ? 24.608 9.457   -3.793  1.00 38.06  ? 286 LYS   A O   1 
ATOM   759  C  CB  . LYS   A 1 107 ? 22.931 11.068  -1.778  1.00 37.73  ? 286 LYS   A CB  1 
ATOM   760  C  CG  . LYS   A 1 107 ? 22.301 12.403  -1.399  1.00 39.00  ? 286 LYS   A CG  1 
ATOM   761  C  CD  . LYS   A 1 107 ? 22.276 12.647  0.094   1.00 39.30  ? 286 LYS   A CD  1 
ATOM   762  C  CE  . LYS   A 1 107 ? 21.580 13.934  0.488   1.00 39.48  ? 286 LYS   A CE  1 
ATOM   763  N  NZ  . LYS   A 1 107 ? 22.377 15.127  0.118   1.00 39.84  ? 286 LYS   A NZ  1 
ATOM   764  N  N   . LEU   A 1 108 ? 22.746 8.179   -3.734  1.00 37.92  ? 287 LEU   A N   1 
ATOM   765  C  CA  . LEU   A 1 108 ? 23.387 6.981   -4.253  1.00 39.43  ? 287 LEU   A CA  1 
ATOM   766  C  C   . LEU   A 1 108 ? 23.335 7.012   -5.778  1.00 40.16  ? 287 LEU   A C   1 
ATOM   767  O  O   . LEU   A 1 108 ? 22.368 6.549   -6.381  1.00 40.05  ? 287 LEU   A O   1 
ATOM   768  C  CB  . LEU   A 1 108 ? 22.682 5.737   -3.702  1.00 39.13  ? 287 LEU   A CB  1 
ATOM   769  C  CG  . LEU   A 1 108 ? 22.962 5.401   -2.237  1.00 40.21  ? 287 LEU   A CG  1 
ATOM   770  C  CD1 . LEU   A 1 108 ? 22.234 4.129   -1.828  1.00 39.70  ? 287 LEU   A CD1 1 
ATOM   771  C  CD2 . LEU   A 1 108 ? 24.455 5.260   -1.982  1.00 39.98  ? 287 LEU   A CD2 1 
ATOM   772  N  N   . GLY   A 1 109 ? 24.391 7.569   -6.382  1.00 41.34  ? 288 GLY   A N   1 
ATOM   773  C  CA  . GLY   A 1 109 ? 24.437 7.796   -7.816  1.00 42.51  ? 288 GLY   A CA  1 
ATOM   774  C  C   . GLY   A 1 109 ? 23.254 8.642   -8.278  1.00 43.01  ? 288 GLY   A C   1 
ATOM   775  O  O   . GLY   A 1 109 ? 22.977 9.693   -7.702  1.00 43.32  ? 288 GLY   A O   1 
ATOM   776  N  N   . SER   A 1 110 ? 22.559 8.154   -9.310  1.00 44.16  ? 289 SER   A N   1 
ATOM   777  C  CA  . SER   A 1 110 ? 21.384 8.816   -9.851  1.00 44.56  ? 289 SER   A CA  1 
ATOM   778  C  C   . SER   A 1 110 ? 20.139 7.965   -9.599  1.00 43.76  ? 289 SER   A C   1 
ATOM   779  O  O   . SER   A 1 110 ? 19.112 8.149   -10.251 1.00 43.03  ? 289 SER   A O   1 
ATOM   780  C  CB  . SER   A 1 110 ? 21.567 9.109   -11.321 1.00 46.51  ? 289 SER   A CB  1 
ATOM   781  O  OG  . SER   A 1 110 ? 21.773 7.908   -12.052 1.00 47.85  ? 289 SER   A OG  1 
ATOM   782  N  N   . TYR   A 1 111 ? 20.243 7.044   -8.633  1.00 41.92  ? 290 TYR   A N   1 
ATOM   783  C  CA  . TYR   A 1 111 ? 19.176 6.100   -8.346  1.00 41.03  ? 290 TYR   A CA  1 
ATOM   784  C  C   . TYR   A 1 111 ? 18.071 6.767   -7.535  1.00 40.50  ? 290 TYR   A C   1 
ATOM   785  O  O   . TYR   A 1 111 ? 18.320 7.705   -6.781  1.00 39.61  ? 290 TYR   A O   1 
ATOM   786  C  CB  . TYR   A 1 111 ? 19.711 4.874   -7.600  1.00 40.62  ? 290 TYR   A CB  1 
ATOM   787  C  CG  . TYR   A 1 111 ? 20.634 3.996   -8.405  1.00 40.97  ? 290 TYR   A CG  1 
ATOM   788  C  CD1 . TYR   A 1 111 ? 20.250 3.498   -9.643  1.00 40.47  ? 290 TYR   A CD1 1 
ATOM   789  C  CD2 . TYR   A 1 111 ? 21.889 3.654   -7.926  1.00 41.06  ? 290 TYR   A CD2 1 
ATOM   790  C  CE1 . TYR   A 1 111 ? 21.092 2.688   -10.388 1.00 40.10  ? 290 TYR   A CE1 1 
ATOM   791  C  CE2 . TYR   A 1 111 ? 22.743 2.845   -8.660  1.00 40.88  ? 290 TYR   A CE2 1 
ATOM   792  C  CZ  . TYR   A 1 111 ? 22.343 2.360   -9.893  1.00 40.62  ? 290 TYR   A CZ  1 
ATOM   793  O  OH  . TYR   A 1 111 ? 23.186 1.558   -10.618 1.00 41.74  ? 290 TYR   A OH  1 
ATOM   794  N  N   . LYS   A 1 112 ? 16.847 6.259   -7.719  1.00 40.21  ? 291 LYS   A N   1 
ATOM   795  C  CA  . LYS   A 1 112 ? 15.709 6.596   -6.882  1.00 40.78  ? 291 LYS   A CA  1 
ATOM   796  C  C   . LYS   A 1 112 ? 15.131 5.298   -6.323  1.00 39.48  ? 291 LYS   A C   1 
ATOM   797  O  O   . LYS   A 1 112 ? 14.426 4.576   -7.025  1.00 37.09  ? 291 LYS   A O   1 
ATOM   798  C  CB  . LYS   A 1 112 ? 14.672 7.399   -7.677  1.00 42.85  ? 291 LYS   A CB  1 
ATOM   799  C  CG  . LYS   A 1 112 ? 15.175 8.691   -8.311  1.00 46.36  ? 291 LYS   A CG  1 
ATOM   800  C  CD  . LYS   A 1 112 ? 15.650 9.727   -7.309  1.00 48.80  ? 291 LYS   A CD  1 
ATOM   801  C  CE  . LYS   A 1 112 ? 16.128 11.008  -7.958  1.00 50.51  ? 291 LYS   A CE  1 
ATOM   802  N  NZ  . LYS   A 1 112 ? 16.590 11.994  -6.952  1.00 52.02  ? 291 LYS   A NZ  1 
ATOM   803  N  N   . ILE   A 1 113 ? 15.469 5.005   -5.060  1.00 39.71  ? 292 ILE   A N   1 
ATOM   804  C  CA  . ILE   A 1 113 ? 15.047 3.786   -4.386  1.00 39.83  ? 292 ILE   A CA  1 
ATOM   805  C  C   . ILE   A 1 113 ? 13.586 3.943   -3.975  1.00 39.27  ? 292 ILE   A C   1 
ATOM   806  O  O   . ILE   A 1 113 ? 13.240 4.910   -3.302  1.00 40.70  ? 292 ILE   A O   1 
ATOM   807  C  CB  . ILE   A 1 113 ? 15.932 3.496   -3.155  1.00 40.84  ? 292 ILE   A CB  1 
ATOM   808  C  CG1 . ILE   A 1 113 ? 17.425 3.724   -3.415  1.00 41.80  ? 292 ILE   A CG1 1 
ATOM   809  C  CG2 . ILE   A 1 113 ? 15.644 2.109   -2.598  1.00 41.18  ? 292 ILE   A CG2 1 
ATOM   810  C  CD1 . ILE   A 1 113 ? 18.089 2.666   -4.264  1.00 41.64  ? 292 ILE   A CD1 1 
ATOM   811  N  N   . ASN   A 1 114 ? 12.746 2.972   -4.357  1.00 38.72  ? 293 ASN   A N   1 
ATOM   812  C  CA  . ASN   A 1 114 ? 11.325 3.049   -4.053  1.00 39.79  ? 293 ASN   A CA  1 
ATOM   813  C  C   . ASN   A 1 114 ? 10.812 1.734   -3.466  1.00 38.56  ? 293 ASN   A C   1 
ATOM   814  O  O   . ASN   A 1 114 ? 9.637  1.634   -3.111  1.00 39.48  ? 293 ASN   A O   1 
ATOM   815  C  CB  . ASN   A 1 114 ? 10.489 3.523   -5.250  1.00 40.16  ? 293 ASN   A CB  1 
ATOM   816  C  CG  . ASN   A 1 114 ? 10.341 2.502   -6.361  1.00 41.11  ? 293 ASN   A CG  1 
ATOM   817  O  OD1 . ASN   A 1 114 ? 9.363  2.539   -7.107  1.00 41.68  ? 293 ASN   A OD1 1 
ATOM   818  N  ND2 . ASN   A 1 114 ? 11.283 1.579   -6.479  1.00 41.20  ? 293 ASN   A ND2 1 
ATOM   819  N  N   . GLY   A 1 115 ? 11.692 0.731   -3.368  1.00 35.94  ? 294 GLY   A N   1 
ATOM   820  C  CA  . GLY   A 1 115 ? 11.307 -0.568  -2.840  1.00 32.93  ? 294 GLY   A CA  1 
ATOM   821  C  C   . GLY   A 1 115 ? 12.499 -1.513  -2.709  1.00 31.10  ? 294 GLY   A C   1 
ATOM   822  O  O   . GLY   A 1 115 ? 13.628 -1.141  -3.020  1.00 29.98  ? 294 GLY   A O   1 
ATOM   823  N  N   . ARG   A 1 116 ? 12.222 -2.736  -2.240  1.00 29.49  ? 295 ARG   A N   1 
ATOM   824  C  CA  . ARG   A 1 116 ? 13.236 -3.769  -2.097  1.00 28.56  ? 295 ARG   A CA  1 
ATOM   825  C  C   . ARG   A 1 116 ? 12.589 -5.150  -2.168  1.00 27.83  ? 295 ARG   A C   1 
ATOM   826  O  O   . ARG   A 1 116 ? 11.364 -5.274  -2.191  1.00 27.59  ? 295 ARG   A O   1 
ATOM   827  C  CB  . ARG   A 1 116 ? 14.003 -3.603  -0.780  1.00 28.22  ? 295 ARG   A CB  1 
ATOM   828  C  CG  . ARG   A 1 116 ? 13.136 -3.689  0.469   1.00 28.86  ? 295 ARG   A CG  1 
ATOM   829  C  CD  . ARG   A 1 116 ? 13.939 -4.077  1.697   1.00 29.39  ? 295 ARG   A CD  1 
ATOM   830  N  NE  . ARG   A 1 116 ? 13.179 -3.937  2.934   1.00 29.29  ? 295 ARG   A NE  1 
ATOM   831  C  CZ  . ARG   A 1 116 ? 12.184 -4.727  3.328   1.00 29.69  ? 295 ARG   A CZ  1 
ATOM   832  N  NH1 . ARG   A 1 116 ? 11.549 -4.469  4.458   1.00 28.90  ? 295 ARG   A NH1 1 
ATOM   833  N  NH2 . ARG   A 1 116 ? 11.824 -5.770  2.599   1.00 28.76  ? 295 ARG   A NH2 1 
ATOM   834  N  N   . THR   A 1 117 ? 13.441 -6.180  -2.200  1.00 26.83  ? 296 THR   A N   1 
ATOM   835  C  CA  . THR   A 1 117 ? 13.021 -7.567  -2.102  1.00 26.25  ? 296 THR   A CA  1 
ATOM   836  C  C   . THR   A 1 117 ? 12.714 -7.885  -0.639  1.00 26.52  ? 296 THR   A C   1 
ATOM   837  O  O   . THR   A 1 117 ? 12.980 -7.078  0.250   1.00 25.92  ? 296 THR   A O   1 
ATOM   838  C  CB  . THR   A 1 117 ? 14.128 -8.501  -2.614  1.00 26.36  ? 296 THR   A CB  1 
ATOM   839  O  OG1 . THR   A 1 117 ? 15.277 -8.350  -1.776  1.00 26.21  ? 296 THR   A OG1 1 
ATOM   840  C  CG2 . THR   A 1 117 ? 14.525 -8.231  -4.048  1.00 26.21  ? 296 THR   A CG2 1 
ATOM   841  N  N   . LYS   A 1 118 ? 12.157 -9.077  -0.397  1.00 26.45  ? 297 LYS   A N   1 
ATOM   842  C  CA  . LYS   A 1 118 ? 12.186 -9.660  0.933   1.00 27.12  ? 297 LYS   A CA  1 
ATOM   843  C  C   . LYS   A 1 118 ? 13.636 -10.026 1.250   1.00 26.28  ? 297 LYS   A C   1 
ATOM   844  O  O   . LYS   A 1 118 ? 14.517 -9.848  0.412   1.00 26.59  ? 297 LYS   A O   1 
ATOM   845  C  CB  . LYS   A 1 118 ? 11.265 -10.882 1.002   1.00 29.04  ? 297 LYS   A CB  1 
ATOM   846  C  CG  . LYS   A 1 118 ? 9.775  -10.596 0.857   1.00 30.74  ? 297 LYS   A CG  1 
ATOM   847  C  CD  . LYS   A 1 118 ? 8.936  -11.854 0.949   1.00 32.67  ? 297 LYS   A CD  1 
ATOM   848  C  CE  . LYS   A 1 118 ? 7.448  -11.616 0.791   1.00 34.38  ? 297 LYS   A CE  1 
ATOM   849  N  NZ  . LYS   A 1 118 ? 7.096  -11.220 -0.592  1.00 36.33  ? 297 LYS   A NZ  1 
ATOM   850  N  N   . ALA   A 1 119 ? 13.880 -10.529 2.464   1.00 25.90  ? 298 ALA   A N   1 
ATOM   851  C  CA  . ALA   A 1 119 ? 15.224 -10.917 2.858   1.00 25.95  ? 298 ALA   A CA  1 
ATOM   852  C  C   . ALA   A 1 119 ? 15.501 -12.356 2.430   1.00 26.11  ? 298 ALA   A C   1 
ATOM   853  O  O   . ALA   A 1 119 ? 14.712 -13.258 2.708   1.00 26.62  ? 298 ALA   A O   1 
ATOM   854  C  CB  . ALA   A 1 119 ? 15.406 -10.736 4.344   1.00 25.15  ? 298 ALA   A CB  1 
ATOM   855  N  N   . MET   A 1 120 ? 16.631 -12.550 1.747   1.00 26.32  ? 299 MET   A N   1 
ATOM   856  C  CA  . MET   A 1 120 ? 17.103 -13.886 1.430   1.00 26.98  ? 299 MET   A CA  1 
ATOM   857  C  C   . MET   A 1 120 ? 18.107 -14.309 2.500   1.00 26.48  ? 299 MET   A C   1 
ATOM   858  O  O   . MET   A 1 120 ? 19.220 -13.783 2.570   1.00 26.28  ? 299 MET   A O   1 
ATOM   859  C  CB  . MET   A 1 120 ? 17.765 -13.937 0.048   1.00 28.25  ? 299 MET   A CB  1 
ATOM   860  C  CG  . MET   A 1 120 ? 18.357 -15.298 -0.285  1.00 29.79  ? 299 MET   A CG  1 
ATOM   861  S  SD  . MET   A 1 120 ? 19.325 -15.301 -1.813  1.00 32.21  ? 299 MET   A SD  1 
ATOM   862  C  CE  . MET   A 1 120 ? 20.888 -14.686 -1.184  1.00 30.81  ? 299 MET   A CE  1 
ATOM   863  N  N   . VAL   A 1 121 ? 17.683 -15.252 3.345   1.00 26.26  ? 300 VAL   A N   1 
ATOM   864  C  CA  . VAL   A 1 121 ? 18.555 -15.843 4.346   1.00 26.43  ? 300 VAL   A CA  1 
ATOM   865  C  C   . VAL   A 1 121 ? 19.308 -16.983 3.670   1.00 26.19  ? 300 VAL   A C   1 
ATOM   866  O  O   . VAL   A 1 121 ? 18.692 -17.879 3.101   1.00 24.97  ? 300 VAL   A O   1 
ATOM   867  C  CB  . VAL   A 1 121 ? 17.756 -16.334 5.570   1.00 26.73  ? 300 VAL   A CB  1 
ATOM   868  C  CG1 . VAL   A 1 121 ? 18.666 -16.917 6.644   1.00 26.33  ? 300 VAL   A CG1 1 
ATOM   869  C  CG2 . VAL   A 1 121 ? 16.886 -15.231 6.153   1.00 27.09  ? 300 VAL   A CG2 1 
ATOM   870  N  N   . ALA   A 1 122 ? 20.644 -16.924 3.713   1.00 26.25  ? 301 ALA   A N   1 
ATOM   871  C  CA  . ALA   A 1 122 ? 21.456 -17.926 3.044   1.00 26.18  ? 301 ALA   A CA  1 
ATOM   872  C  C   . ALA   A 1 122 ? 22.294 -18.693 4.062   1.00 26.56  ? 301 ALA   A C   1 
ATOM   873  O  O   . ALA   A 1 122 ? 22.812 -18.116 5.018   1.00 27.22  ? 301 ALA   A O   1 
ATOM   874  C  CB  . ALA   A 1 122 ? 22.317 -17.290 1.977   1.00 26.01  ? 301 ALA   A CB  1 
ATOM   875  N  N   . CYS   A 1 123 ? 22.415 -20.002 3.825   1.00 26.83  ? 302 CYS   A N   1 
ATOM   876  C  CA  . CYS   A 1 123 ? 23.216 -20.886 4.652   1.00 28.05  ? 302 CYS   A CA  1 
ATOM   877  C  C   . CYS   A 1 123 ? 24.183 -21.666 3.764   1.00 28.20  ? 302 CYS   A C   1 
ATOM   878  O  O   . CYS   A 1 123 ? 23.760 -22.342 2.831   1.00 27.85  ? 302 CYS   A O   1 
ATOM   879  C  CB  . CYS   A 1 123 ? 22.322 -21.856 5.418   1.00 29.12  ? 302 CYS   A CB  1 
ATOM   880  S  SG  . CYS   A 1 123 ? 23.241 -23.067 6.405   1.00 31.28  ? 302 CYS   A SG  1 
ATOM   881  N  N   . TYR   A 1 124 ? 25.484 -21.533 4.052   1.00 28.74  ? 303 TYR   A N   1 
ATOM   882  C  CA  . TYR   A 1 124 ? 26.500 -22.404 3.484   1.00 30.22  ? 303 TYR   A CA  1 
ATOM   883  C  C   . TYR   A 1 124 ? 26.902 -23.412 4.554   1.00 31.46  ? 303 TYR   A C   1 
ATOM   884  O  O   . TYR   A 1 124 ? 27.552 -23.047 5.533   1.00 30.85  ? 303 TYR   A O   1 
ATOM   885  C  CB  . TYR   A 1 124 ? 27.702 -21.606 2.971   1.00 30.39  ? 303 TYR   A CB  1 
ATOM   886  C  CG  . TYR   A 1 124 ? 27.402 -20.655 1.839   1.00 30.74  ? 303 TYR   A CG  1 
ATOM   887  C  CD1 . TYR   A 1 124 ? 26.795 -19.429 2.069   1.00 30.48  ? 303 TYR   A CD1 1 
ATOM   888  C  CD2 . TYR   A 1 124 ? 27.713 -20.991 0.530   1.00 31.44  ? 303 TYR   A CD2 1 
ATOM   889  C  CE1 . TYR   A 1 124 ? 26.513 -18.553 1.030   1.00 31.16  ? 303 TYR   A CE1 1 
ATOM   890  C  CE2 . TYR   A 1 124 ? 27.441 -20.127 -0.519  1.00 31.98  ? 303 TYR   A CE2 1 
ATOM   891  C  CZ  . TYR   A 1 124 ? 26.840 -18.905 -0.269  1.00 31.73  ? 303 TYR   A CZ  1 
ATOM   892  O  OH  . TYR   A 1 124 ? 26.569 -18.056 -1.314  1.00 32.55  ? 303 TYR   A OH  1 
ATOM   893  N  N   . PRO   A 1 125 ? 26.520 -24.701 4.404   1.00 33.59  ? 304 PRO   A N   1 
ATOM   894  C  CA  . PRO   A 1 125 ? 26.582 -25.662 5.508   1.00 35.93  ? 304 PRO   A CA  1 
ATOM   895  C  C   . PRO   A 1 125 ? 27.992 -26.154 5.820   1.00 38.51  ? 304 PRO   A C   1 
ATOM   896  O  O   . PRO   A 1 125 ? 28.166 -27.260 6.329   1.00 41.19  ? 304 PRO   A O   1 
ATOM   897  C  CB  . PRO   A 1 125 ? 25.719 -26.821 4.984   1.00 35.28  ? 304 PRO   A CB  1 
ATOM   898  C  CG  . PRO   A 1 125 ? 25.920 -26.780 3.487   1.00 34.26  ? 304 PRO   A CG  1 
ATOM   899  C  CD  . PRO   A 1 125 ? 26.018 -25.305 3.158   1.00 34.35  ? 304 PRO   A CD  1 
ATOM   900  N  N   . GLY   A 1 126 ? 28.991 -25.315 5.527   1.00 39.05  ? 305 GLY   A N   1 
ATOM   901  C  CA  . GLY   A 1 126 ? 30.383 -25.714 5.623   1.00 40.70  ? 305 GLY   A CA  1 
ATOM   902  C  C   . GLY   A 1 126 ? 30.699 -26.796 4.594   1.00 42.89  ? 305 GLY   A C   1 
ATOM   903  O  O   . GLY   A 1 126 ? 30.005 -26.914 3.586   1.00 44.04  ? 305 GLY   A O   1 
ATOM   904  N  N   . ASN   A 1 127 ? 31.749 -27.577 4.870   1.00 42.59  ? 306 ASN   A N   1 
ATOM   905  C  CA  . ASN   A 1 127 ? 32.131 -28.707 4.037   1.00 43.43  ? 306 ASN   A CA  1 
ATOM   906  C  C   . ASN   A 1 127 ? 32.488 -28.233 2.628   1.00 41.06  ? 306 ASN   A C   1 
ATOM   907  O  O   . ASN   A 1 127 ? 32.177 -28.901 1.644   1.00 41.01  ? 306 ASN   A O   1 
ATOM   908  C  CB  . ASN   A 1 127 ? 31.075 -29.819 4.067   1.00 46.83  ? 306 ASN   A CB  1 
ATOM   909  C  CG  . ASN   A 1 127 ? 30.875 -30.417 5.445   1.00 50.04  ? 306 ASN   A CG  1 
ATOM   910  O  OD1 . ASN   A 1 127 ? 29.795 -30.313 6.023   1.00 50.99  ? 306 ASN   A OD1 1 
ATOM   911  N  ND2 . ASN   A 1 127 ? 31.908 -31.049 5.980   1.00 50.90  ? 306 ASN   A ND2 1 
ATOM   912  N  N   . GLY   A 1 128 ? 33.134 -27.064 2.546   1.00 38.69  ? 307 GLY   A N   1 
ATOM   913  C  CA  . GLY   A 1 128 ? 33.752 -26.593 1.316   1.00 38.14  ? 307 GLY   A CA  1 
ATOM   914  C  C   . GLY   A 1 128 ? 32.791 -25.856 0.386   1.00 37.48  ? 307 GLY   A C   1 
ATOM   915  O  O   . GLY   A 1 128 ? 33.177 -25.482 -0.719  1.00 37.66  ? 307 GLY   A O   1 
ATOM   916  N  N   . THR   A 1 129 ? 31.550 -25.642 0.840   1.00 37.86  ? 308 THR   A N   1 
ATOM   917  C  CA  . THR   A 1 129 ? 30.527 -25.016 0.015   1.00 38.51  ? 308 THR   A CA  1 
ATOM   918  C  C   . THR   A 1 129 ? 30.819 -23.525 -0.137  1.00 38.19  ? 308 THR   A C   1 
ATOM   919  O  O   . THR   A 1 129 ? 31.214 -22.861 0.820   1.00 37.84  ? 308 THR   A O   1 
ATOM   920  C  CB  . THR   A 1 129 ? 29.118 -25.246 0.578   1.00 38.80  ? 308 THR   A CB  1 
ATOM   921  O  OG1 . THR   A 1 129 ? 29.073 -24.716 1.904   1.00 40.10  ? 308 THR   A OG1 1 
ATOM   922  C  CG2 . THR   A 1 129 ? 28.708 -26.703 0.577   1.00 38.05  ? 308 THR   A CG2 1 
ATOM   923  N  N   . GLY   A 1 130 ? 30.615 -23.022 -1.360  1.00 37.30  ? 309 GLY   A N   1 
ATOM   924  C  CA  . GLY   A 1 130 ? 30.781 -21.613 -1.680  1.00 35.75  ? 309 GLY   A CA  1 
ATOM   925  C  C   . GLY   A 1 130 ? 29.859 -21.188 -2.820  1.00 34.63  ? 309 GLY   A C   1 
ATOM   926  O  O   . GLY   A 1 130 ? 28.830 -21.819 -3.060  1.00 33.97  ? 309 GLY   A O   1 
ATOM   927  N  N   . TYR   A 1 131 ? 30.246 -20.111 -3.513  1.00 33.09  ? 310 TYR   A N   1 
ATOM   928  C  CA  . TYR   A 1 131 ? 29.482 -19.590 -4.635  1.00 32.98  ? 310 TYR   A CA  1 
ATOM   929  C  C   . TYR   A 1 131 ? 30.452 -18.985 -5.646  1.00 31.91  ? 310 TYR   A C   1 
ATOM   930  O  O   . TYR   A 1 131 ? 31.262 -18.127 -5.293  1.00 30.89  ? 310 TYR   A O   1 
ATOM   931  C  CB  . TYR   A 1 131 ? 28.460 -18.560 -4.143  1.00 34.78  ? 310 TYR   A CB  1 
ATOM   932  C  CG  . TYR   A 1 131 ? 27.250 -18.371 -5.024  1.00 36.53  ? 310 TYR   A CG  1 
ATOM   933  C  CD1 . TYR   A 1 131 ? 27.361 -17.867 -6.311  1.00 37.88  ? 310 TYR   A CD1 1 
ATOM   934  C  CD2 . TYR   A 1 131 ? 25.984 -18.699 -4.567  1.00 39.27  ? 310 TYR   A CD2 1 
ATOM   935  C  CE1 . TYR   A 1 131 ? 26.248 -17.691 -7.119  1.00 39.82  ? 310 TYR   A CE1 1 
ATOM   936  C  CE2 . TYR   A 1 131 ? 24.861 -18.535 -5.362  1.00 40.75  ? 310 TYR   A CE2 1 
ATOM   937  C  CZ  . TYR   A 1 131 ? 24.992 -18.027 -6.643  1.00 41.47  ? 310 TYR   A CZ  1 
ATOM   938  O  OH  . TYR   A 1 131 ? 23.880 -17.862 -7.433  1.00 44.31  ? 310 TYR   A OH  1 
ATOM   939  N  N   . VAL   A 1 132 ? 30.356 -19.445 -6.901  1.00 30.63  ? 311 VAL   A N   1 
ATOM   940  C  CA  . VAL   A 1 132 ? 31.270 -19.034 -7.957  1.00 30.89  ? 311 VAL   A CA  1 
ATOM   941  C  C   . VAL   A 1 132 ? 31.045 -17.559 -8.284  1.00 30.07  ? 311 VAL   A C   1 
ATOM   942  O  O   . VAL   A 1 132 ? 29.997 -16.995 -7.970  1.00 29.48  ? 311 VAL   A O   1 
ATOM   943  C  CB  . VAL   A 1 132 ? 31.145 -19.911 -9.222  1.00 32.02  ? 311 VAL   A CB  1 
ATOM   944  C  CG1 . VAL   A 1 132 ? 31.540 -21.357 -8.959  1.00 32.03  ? 311 VAL   A CG1 1 
ATOM   945  C  CG2 . VAL   A 1 132 ? 29.758 -19.830 -9.844  1.00 32.15  ? 311 VAL   A CG2 1 
ATOM   946  N  N   . ARG   A 1 133 ? 32.053 -16.956 -8.923  1.00 28.65  ? 312 ARG   A N   1 
ATOM   947  C  CA  . ARG   A 1 133 ? 32.013 -15.571 -9.357  1.00 29.36  ? 312 ARG   A CA  1 
ATOM   948  C  C   . ARG   A 1 133 ? 30.731 -15.327 -10.152 1.00 28.47  ? 312 ARG   A C   1 
ATOM   949  O  O   . ARG   A 1 133 ? 30.409 -16.088 -11.064 1.00 27.78  ? 312 ARG   A O   1 
ATOM   950  C  CB  . ARG   A 1 133 ? 33.267 -15.275 -10.184 1.00 30.75  ? 312 ARG   A CB  1 
ATOM   951  C  CG  . ARG   A 1 133 ? 33.554 -13.798 -10.402 1.00 32.69  ? 312 ARG   A CG  1 
ATOM   952  C  CD  . ARG   A 1 133 ? 34.823 -13.661 -11.219 1.00 35.25  ? 312 ARG   A CD  1 
ATOM   953  N  NE  . ARG   A 1 133 ? 35.078 -12.302 -11.672 1.00 37.05  ? 312 ARG   A NE  1 
ATOM   954  C  CZ  . ARG   A 1 133 ? 36.239 -11.669 -11.546 1.00 37.73  ? 312 ARG   A CZ  1 
ATOM   955  N  NH1 . ARG   A 1 133 ? 37.269 -12.270 -10.975 1.00 36.92  ? 312 ARG   A NH1 1 
ATOM   956  N  NH2 . ARG   A 1 133 ? 36.364 -10.434 -12.001 1.00 38.96  ? 312 ARG   A NH2 1 
ATOM   957  N  N   . HIS   A 1 134 ? 29.999 -14.271 -9.777  1.00 27.53  ? 313 HIS   A N   1 
ATOM   958  C  CA  . HIS   A 1 134 ? 28.737 -13.920 -10.408 1.00 28.00  ? 313 HIS   A CA  1 
ATOM   959  C  C   . HIS   A 1 134 ? 28.431 -12.438 -10.195 1.00 28.82  ? 313 HIS   A C   1 
ATOM   960  O  O   . HIS   A 1 134 ? 29.018 -11.786 -9.330  1.00 27.64  ? 313 HIS   A O   1 
ATOM   961  C  CB  . HIS   A 1 134 ? 27.588 -14.753 -9.821  1.00 27.66  ? 313 HIS   A CB  1 
ATOM   962  C  CG  . HIS   A 1 134 ? 27.328 -14.457 -8.379  1.00 27.16  ? 313 HIS   A CG  1 
ATOM   963  N  ND1 . HIS   A 1 134 ? 28.121 -14.936 -7.360  1.00 27.13  ? 313 HIS   A ND1 1 
ATOM   964  C  CD2 . HIS   A 1 134 ? 26.369 -13.729 -7.791  1.00 27.41  ? 313 HIS   A CD2 1 
ATOM   965  C  CE1 . HIS   A 1 134 ? 27.649 -14.503 -6.198  1.00 27.93  ? 313 HIS   A CE1 1 
ATOM   966  N  NE2 . HIS   A 1 134 ? 26.589 -13.766 -6.438  1.00 26.64  ? 313 HIS   A NE2 1 
ATOM   967  N  N   . VAL   A 1 135 ? 27.488 -11.930 -10.997 1.00 29.31  ? 314 VAL   A N   1 
ATOM   968  C  CA  . VAL   A 1 135 ? 26.882 -10.622 -10.802 1.00 29.22  ? 314 VAL   A CA  1 
ATOM   969  C  C   . VAL   A 1 135 ? 25.435 -10.834 -10.357 1.00 28.61  ? 314 VAL   A C   1 
ATOM   970  O  O   . VAL   A 1 135 ? 24.727 -11.658 -10.932 1.00 27.88  ? 314 VAL   A O   1 
ATOM   971  C  CB  . VAL   A 1 135 ? 26.979 -9.777  -12.089 1.00 30.50  ? 314 VAL   A CB  1 
ATOM   972  C  CG1 . VAL   A 1 135 ? 26.040 -8.580  -12.080 1.00 30.60  ? 314 VAL   A CG1 1 
ATOM   973  C  CG2 . VAL   A 1 135 ? 28.411 -9.342  -12.373 1.00 29.88  ? 314 VAL   A CG2 1 
ATOM   974  N  N   . ASP   A 1 136 ? 25.014 -10.092 -9.323  1.00 28.08  ? 315 ASP   A N   1 
ATOM   975  C  CA  . ASP   A 1 136 ? 23.672 -10.203 -8.769  1.00 29.53  ? 315 ASP   A CA  1 
ATOM   976  C  C   . ASP   A 1 136 ? 22.625 -9.833  -9.816  1.00 30.27  ? 315 ASP   A C   1 
ATOM   977  O  O   . ASP   A 1 136 ? 21.689 -10.596 -10.046 1.00 30.95  ? 315 ASP   A O   1 
ATOM   978  C  CB  . ASP   A 1 136 ? 23.498 -9.342  -7.516  1.00 28.39  ? 315 ASP   A CB  1 
ATOM   979  C  CG  . ASP   A 1 136 ? 24.075 -9.963  -6.257  1.00 28.03  ? 315 ASP   A CG  1 
ATOM   980  O  OD1 . ASP   A 1 136 ? 24.566 -11.110 -6.332  1.00 27.69  ? 315 ASP   A OD1 1 
ATOM   981  O  OD2 . ASP   A 1 136 ? 24.012 -9.298  -5.208  1.00 27.27  ? 315 ASP   A OD2 1 
ATOM   982  N  N   . ASN   A 1 137 ? 22.791 -8.653  -10.427 1.00 29.77  ? 316 ASN   A N   1 
ATOM   983  C  CA  . ASN   A 1 137 ? 21.851 -8.140  -11.413 1.00 31.05  ? 316 ASN   A CA  1 
ATOM   984  C  C   . ASN   A 1 137 ? 22.602 -7.832  -12.708 1.00 31.57  ? 316 ASN   A C   1 
ATOM   985  O  O   . ASN   A 1 137 ? 23.025 -6.695  -12.923 1.00 30.91  ? 316 ASN   A O   1 
ATOM   986  C  CB  . ASN   A 1 137 ? 21.093 -6.916  -10.885 1.00 30.97  ? 316 ASN   A CB  1 
ATOM   987  C  CG  . ASN   A 1 137 ? 20.179 -6.268  -11.906 1.00 31.64  ? 316 ASN   A CG  1 
ATOM   988  O  OD1 . ASN   A 1 137 ? 19.837 -6.869  -12.924 1.00 31.74  ? 316 ASN   A OD1 1 
ATOM   989  N  ND2 . ASN   A 1 137 ? 19.762 -5.042  -11.636 1.00 31.26  ? 316 ASN   A ND2 1 
ATOM   990  N  N   . PRO   A 1 138 ? 22.811 -8.831  -13.600 1.00 32.45  ? 317 PRO   A N   1 
ATOM   991  C  CA  . PRO   A 1 138 ? 23.451 -8.586  -14.893 1.00 34.38  ? 317 PRO   A CA  1 
ATOM   992  C  C   . PRO   A 1 138 ? 22.523 -8.143  -16.026 1.00 35.90  ? 317 PRO   A C   1 
ATOM   993  O  O   . PRO   A 1 138 ? 22.998 -7.632  -17.036 1.00 35.50  ? 317 PRO   A O   1 
ATOM   994  C  CB  . PRO   A 1 138 ? 24.052 -9.962  -15.215 1.00 33.72  ? 317 PRO   A CB  1 
ATOM   995  C  CG  . PRO   A 1 138 ? 23.067 -10.945 -14.617 1.00 33.46  ? 317 PRO   A CG  1 
ATOM   996  C  CD  . PRO   A 1 138 ? 22.512 -10.257 -13.385 1.00 33.28  ? 317 PRO   A CD  1 
ATOM   997  N  N   . ASN   A 1 139 ? 21.207 -8.329  -15.851 1.00 37.90  ? 318 ASN   A N   1 
ATOM   998  C  CA  . ASN   A 1 139 ? 20.260 -8.147  -16.944 1.00 39.64  ? 318 ASN   A CA  1 
ATOM   999  C  C   . ASN   A 1 139 ? 19.298 -6.988  -16.667 1.00 39.29  ? 318 ASN   A C   1 
ATOM   1000 O  O   . ASN   A 1 139 ? 18.228 -6.917  -17.271 1.00 38.82  ? 318 ASN   A O   1 
ATOM   1001 C  CB  . ASN   A 1 139 ? 19.515 -9.446  -17.273 1.00 41.88  ? 318 ASN   A CB  1 
ATOM   1002 C  CG  . ASN   A 1 139 ? 20.433 -10.594 -17.644 1.00 43.96  ? 318 ASN   A CG  1 
ATOM   1003 O  OD1 . ASN   A 1 139 ? 20.473 -11.610 -16.952 1.00 46.40  ? 318 ASN   A OD1 1 
ATOM   1004 N  ND2 . ASN   A 1 139 ? 21.174 -10.447 -18.731 1.00 43.33  ? 318 ASN   A ND2 1 
ATOM   1005 N  N   . GLY   A 1 140 ? 19.687 -6.084  -15.758 1.00 38.14  ? 319 GLY   A N   1 
ATOM   1006 C  CA  . GLY   A 1 140 ? 18.937 -4.870  -15.462 1.00 36.85  ? 319 GLY   A CA  1 
ATOM   1007 C  C   . GLY   A 1 140 ? 17.502 -5.139  -15.009 1.00 35.59  ? 319 GLY   A C   1 
ATOM   1008 O  O   . GLY   A 1 140 ? 16.556 -4.660  -15.632 1.00 33.97  ? 319 GLY   A O   1 
ATOM   1009 N  N   . ASP   A 1 141 ? 17.350 -5.878  -13.904 1.00 35.11  ? 320 ASP   A N   1 
ATOM   1010 C  CA  . ASP   A 1 141 ? 16.032 -6.267  -13.421 1.00 34.75  ? 320 ASP   A CA  1 
ATOM   1011 C  C   . ASP   A 1 141 ? 15.509 -5.266  -12.387 1.00 33.24  ? 320 ASP   A C   1 
ATOM   1012 O  O   . ASP   A 1 141 ? 14.436 -5.468  -11.821 1.00 33.84  ? 320 ASP   A O   1 
ATOM   1013 C  CB  . ASP   A 1 141 ? 16.015 -7.719  -12.926 1.00 36.08  ? 320 ASP   A CB  1 
ATOM   1014 C  CG  . ASP   A 1 141 ? 16.790 -7.965  -11.640 1.00 37.94  ? 320 ASP   A CG  1 
ATOM   1015 O  OD1 . ASP   A 1 141 ? 17.470 -7.034  -11.170 1.00 36.95  ? 320 ASP   A OD1 1 
ATOM   1016 O  OD2 . ASP   A 1 141 ? 16.689 -9.088  -11.104 1.00 39.80  ? 320 ASP   A OD2 1 
ATOM   1017 N  N   . GLY   A 1 142 ? 16.273 -4.196  -12.133 1.00 31.50  ? 321 GLY   A N   1 
ATOM   1018 C  CA  . GLY   A 1 142 ? 15.814 -3.126  -11.259 1.00 30.34  ? 321 GLY   A CA  1 
ATOM   1019 C  C   . GLY   A 1 142 ? 16.615 -3.005  -9.963  1.00 29.54  ? 321 GLY   A C   1 
ATOM   1020 O  O   . GLY   A 1 142 ? 16.621 -1.943  -9.344  1.00 29.71  ? 321 GLY   A O   1 
ATOM   1021 N  N   . ARG   A 1 143 ? 17.280 -4.095  -9.559  1.00 28.40  ? 322 ARG   A N   1 
ATOM   1022 C  CA  . ARG   A 1 143 ? 18.020 -4.141  -8.305  1.00 28.44  ? 322 ARG   A CA  1 
ATOM   1023 C  C   . ARG   A 1 143 ? 19.334 -3.379  -8.457  1.00 28.15  ? 322 ARG   A C   1 
ATOM   1024 O  O   . ARG   A 1 143 ? 20.156 -3.739  -9.296  1.00 27.60  ? 322 ARG   A O   1 
ATOM   1025 C  CB  . ARG   A 1 143 ? 18.267 -5.596  -7.893  1.00 28.26  ? 322 ARG   A CB  1 
ATOM   1026 C  CG  . ARG   A 1 143 ? 16.994 -6.365  -7.569  1.00 29.24  ? 322 ARG   A CG  1 
ATOM   1027 C  CD  . ARG   A 1 143 ? 17.198 -7.834  -7.246  1.00 29.63  ? 322 ARG   A CD  1 
ATOM   1028 N  NE  . ARG   A 1 143 ? 17.638 -8.613  -8.396  1.00 30.25  ? 322 ARG   A NE  1 
ATOM   1029 C  CZ  . ARG   A 1 143 ? 18.694 -9.418  -8.413  1.00 30.37  ? 322 ARG   A CZ  1 
ATOM   1030 N  NH1 . ARG   A 1 143 ? 19.435 -9.574  -7.330  1.00 30.90  ? 322 ARG   A NH1 1 
ATOM   1031 N  NH2 . ARG   A 1 143 ? 19.000 -10.072 -9.519  1.00 30.69  ? 322 ARG   A NH2 1 
ATOM   1032 N  N   . CYS   A 1 144 ? 19.524 -2.338  -7.633  1.00 27.64  ? 323 CYS   A N   1 
ATOM   1033 C  CA  . CYS   A 1 144 ? 20.677 -1.460  -7.777  1.00 27.78  ? 323 CYS   A CA  1 
ATOM   1034 C  C   . CYS   A 1 144 ? 21.664 -1.606  -6.615  1.00 26.92  ? 323 CYS   A C   1 
ATOM   1035 O  O   . CYS   A 1 144 ? 22.867 -1.463  -6.825  1.00 26.83  ? 323 CYS   A O   1 
ATOM   1036 C  CB  . CYS   A 1 144 ? 20.275 -0.005  -8.023  1.00 29.36  ? 323 CYS   A CB  1 
ATOM   1037 S  SG  . CYS   A 1 144 ? 19.303 0.762   -6.697  1.00 33.16  ? 323 CYS   A SG  1 
ATOM   1038 N  N   . VAL   A 1 145 ? 21.165 -1.889  -5.401  1.00 25.68  ? 324 VAL   A N   1 
ATOM   1039 C  CA  . VAL   A 1 145 ? 22.032 -2.019  -4.236  1.00 25.48  ? 324 VAL   A CA  1 
ATOM   1040 C  C   . VAL   A 1 145 ? 21.765 -3.349  -3.528  1.00 25.60  ? 324 VAL   A C   1 
ATOM   1041 O  O   . VAL   A 1 145 ? 20.627 -3.668  -3.188  1.00 25.60  ? 324 VAL   A O   1 
ATOM   1042 C  CB  . VAL   A 1 145 ? 21.904 -0.824  -3.265  1.00 26.02  ? 324 VAL   A CB  1 
ATOM   1043 C  CG1 . VAL   A 1 145 ? 22.725 -1.032  -1.999  1.00 25.91  ? 324 VAL   A CG1 1 
ATOM   1044 C  CG2 . VAL   A 1 145 ? 22.283 0.498   -3.918  1.00 25.13  ? 324 VAL   A CG2 1 
ATOM   1045 N  N   . THR   A 1 146 ? 22.841 -4.116  -3.319  1.00 24.85  ? 325 THR   A N   1 
ATOM   1046 C  CA  . THR   A 1 146 ? 22.815 -5.322  -2.510  1.00 24.42  ? 325 THR   A CA  1 
ATOM   1047 C  C   . THR   A 1 146 ? 23.211 -4.956  -1.082  1.00 25.01  ? 325 THR   A C   1 
ATOM   1048 O  O   . THR   A 1 146 ? 24.221 -4.288  -0.869  1.00 25.26  ? 325 THR   A O   1 
ATOM   1049 C  CB  . THR   A 1 146 ? 23.792 -6.375  -3.053  1.00 24.28  ? 325 THR   A CB  1 
ATOM   1050 O  OG1 . THR   A 1 146 ? 23.481 -6.661  -4.418  1.00 23.49  ? 325 THR   A OG1 1 
ATOM   1051 C  CG2 . THR   A 1 146 ? 23.805 -7.651  -2.239  1.00 23.89  ? 325 THR   A CG2 1 
ATOM   1052 N  N   . CYS   A 1 147 ? 22.414 -5.421  -0.114  1.00 24.88  ? 326 CYS   A N   1 
ATOM   1053 C  CA  . CYS   A 1 147 ? 22.676 -5.175  1.294   1.00 25.76  ? 326 CYS   A CA  1 
ATOM   1054 C  C   . CYS   A 1 147 ? 22.683 -6.508  2.042   1.00 25.46  ? 326 CYS   A C   1 
ATOM   1055 O  O   . CYS   A 1 147 ? 21.663 -7.193  2.087   1.00 24.18  ? 326 CYS   A O   1 
ATOM   1056 C  CB  . CYS   A 1 147 ? 21.611 -4.246  1.868   1.00 27.32  ? 326 CYS   A CB  1 
ATOM   1057 S  SG  . CYS   A 1 147 ? 21.891 -3.812  3.605   1.00 29.22  ? 326 CYS   A SG  1 
ATOM   1058 N  N   . ILE   A 1 148 ? 23.842 -6.860  2.619   1.00 25.24  ? 327 ILE   A N   1 
ATOM   1059 C  CA  . ILE   A 1 148 ? 24.035 -8.141  3.287   1.00 25.40  ? 327 ILE   A CA  1 
ATOM   1060 C  C   . ILE   A 1 148 ? 24.393 -7.906  4.753   1.00 25.27  ? 327 ILE   A C   1 
ATOM   1061 O  O   . ILE   A 1 148 ? 25.213 -7.045  5.067   1.00 26.30  ? 327 ILE   A O   1 
ATOM   1062 C  CB  . ILE   A 1 148 ? 25.118 -8.992  2.588   1.00 24.69  ? 327 ILE   A CB  1 
ATOM   1063 C  CG1 . ILE   A 1 148 ? 24.934 -9.054  1.068   1.00 25.09  ? 327 ILE   A CG1 1 
ATOM   1064 C  CG2 . ILE   A 1 148 ? 25.194 -10.383 3.209   1.00 25.09  ? 327 ILE   A CG2 1 
ATOM   1065 C  CD1 . ILE   A 1 148 ? 26.031 -9.819  0.343   1.00 24.42  ? 327 ILE   A CD1 1 
ATOM   1066 N  N   . TYR   A 1 149 ? 23.776 -8.698  5.637   1.00 24.16  ? 328 TYR   A N   1 
ATOM   1067 C  CA  . TYR   A 1 149 ? 24.087 -8.708  7.056   1.00 24.28  ? 328 TYR   A CA  1 
ATOM   1068 C  C   . TYR   A 1 149 ? 24.609 -10.090 7.446   1.00 24.33  ? 328 TYR   A C   1 
ATOM   1069 O  O   . TYR   A 1 149 ? 24.000 -11.105 7.114   1.00 23.50  ? 328 TYR   A O   1 
ATOM   1070 C  CB  . TYR   A 1 149 ? 22.839 -8.361  7.872   1.00 24.40  ? 328 TYR   A CB  1 
ATOM   1071 C  CG  . TYR   A 1 149 ? 23.040 -8.331  9.367   1.00 24.61  ? 328 TYR   A CG  1 
ATOM   1072 C  CD1 . TYR   A 1 149 ? 23.720 -7.286  9.977   1.00 24.47  ? 328 TYR   A CD1 1 
ATOM   1073 C  CD2 . TYR   A 1 149 ? 22.558 -9.351  10.175  1.00 23.89  ? 328 TYR   A CD2 1 
ATOM   1074 C  CE1 . TYR   A 1 149 ? 23.904 -7.248  11.349  1.00 23.93  ? 328 TYR   A CE1 1 
ATOM   1075 C  CE2 . TYR   A 1 149 ? 22.733 -9.329  11.550  1.00 24.65  ? 328 TYR   A CE2 1 
ATOM   1076 C  CZ  . TYR   A 1 149 ? 23.410 -8.273  12.138  1.00 25.14  ? 328 TYR   A CZ  1 
ATOM   1077 O  OH  . TYR   A 1 149 ? 23.591 -8.239  13.496  1.00 24.52  ? 328 TYR   A OH  1 
ATOM   1078 N  N   . TYR   A 1 150 ? 25.735 -10.114 8.170   1.00 24.62  ? 329 TYR   A N   1 
ATOM   1079 C  CA  . TYR   A 1 150 ? 26.346 -11.357 8.614   1.00 24.80  ? 329 TYR   A CA  1 
ATOM   1080 C  C   . TYR   A 1 150 ? 26.128 -11.532 10.114  1.00 26.10  ? 329 TYR   A C   1 
ATOM   1081 O  O   . TYR   A 1 150 ? 26.079 -10.554 10.862  1.00 25.24  ? 329 TYR   A O   1 
ATOM   1082 C  CB  . TYR   A 1 150 ? 27.835 -11.374 8.263   1.00 24.63  ? 329 TYR   A CB  1 
ATOM   1083 C  CG  . TYR   A 1 150 ? 28.133 -11.241 6.790   1.00 24.72  ? 329 TYR   A CG  1 
ATOM   1084 C  CD1 . TYR   A 1 150 ? 27.930 -12.301 5.919   1.00 23.91  ? 329 TYR   A CD1 1 
ATOM   1085 C  CD2 . TYR   A 1 150 ? 28.608 -10.050 6.264   1.00 24.63  ? 329 TYR   A CD2 1 
ATOM   1086 C  CE1 . TYR   A 1 150 ? 28.207 -12.189 4.567   1.00 24.30  ? 329 TYR   A CE1 1 
ATOM   1087 C  CE2 . TYR   A 1 150 ? 28.886 -9.919  4.911   1.00 24.68  ? 329 TYR   A CE2 1 
ATOM   1088 C  CZ  . TYR   A 1 150 ? 28.682 -10.991 4.059   1.00 24.74  ? 329 TYR   A CZ  1 
ATOM   1089 O  OH  . TYR   A 1 150 ? 28.951 -10.866 2.716   1.00 25.28  ? 329 TYR   A OH  1 
ATOM   1090 N  N   . LEU   A 1 151 ? 26.005 -12.792 10.546  1.00 27.20  ? 330 LEU   A N   1 
ATOM   1091 C  CA  . LEU   A 1 151 ? 25.681 -13.062 11.938  1.00 29.14  ? 330 LEU   A CA  1 
ATOM   1092 C  C   . LEU   A 1 151 ? 26.440 -14.278 12.476  1.00 29.72  ? 330 LEU   A C   1 
ATOM   1093 O  O   . LEU   A 1 151 ? 25.926 -15.024 13.308  1.00 30.35  ? 330 LEU   A O   1 
ATOM   1094 C  CB  . LEU   A 1 151 ? 24.155 -13.120 12.140  1.00 30.24  ? 330 LEU   A CB  1 
ATOM   1095 C  CG  . LEU   A 1 151 ? 23.286 -13.999 11.229  1.00 31.66  ? 330 LEU   A CG  1 
ATOM   1096 C  CD1 . LEU   A 1 151 ? 23.434 -13.678 9.746   1.00 32.31  ? 330 LEU   A CD1 1 
ATOM   1097 C  CD2 . LEU   A 1 151 ? 23.478 -15.486 11.492  1.00 33.00  ? 330 LEU   A CD2 1 
ATOM   1098 N  N   . ASN   A 1 152 ? 27.699 -14.426 12.046  1.00 29.13  ? 331 ASN   A N   1 
ATOM   1099 C  CA  . ASN   A 1 152 ? 28.514 -15.576 12.411  1.00 30.05  ? 331 ASN   A CA  1 
ATOM   1100 C  C   . ASN   A 1 152 ? 29.413 -15.226 13.597  1.00 31.14  ? 331 ASN   A C   1 
ATOM   1101 O  O   . ASN   A 1 152 ? 30.432 -14.563 13.433  1.00 31.29  ? 331 ASN   A O   1 
ATOM   1102 C  CB  . ASN   A 1 152 ? 29.291 -16.108 11.204  1.00 27.79  ? 331 ASN   A CB  1 
ATOM   1103 C  CG  . ASN   A 1 152 ? 28.385 -16.388 10.024  1.00 27.50  ? 331 ASN   A CG  1 
ATOM   1104 O  OD1 . ASN   A 1 152 ? 27.571 -17.308 10.064  1.00 25.57  ? 331 ASN   A OD1 1 
ATOM   1105 N  ND2 . ASN   A 1 152 ? 28.507 -15.584 8.980   1.00 26.95  ? 331 ASN   A ND2 1 
ATOM   1106 N  N   . LYS   A 1 153 ? 29.016 -15.686 14.789  1.00 33.70  ? 332 LYS   A N   1 
ATOM   1107 C  CA  . LYS   A 1 153 ? 29.754 -15.441 16.020  1.00 36.37  ? 332 LYS   A CA  1 
ATOM   1108 C  C   . LYS   A 1 153 ? 31.170 -16.002 15.922  1.00 36.68  ? 332 LYS   A C   1 
ATOM   1109 O  O   . LYS   A 1 153 ? 31.358 -17.169 15.587  1.00 37.53  ? 332 LYS   A O   1 
ATOM   1110 C  CB  . LYS   A 1 153 ? 29.012 -16.031 17.223  1.00 38.76  ? 332 LYS   A CB  1 
ATOM   1111 C  CG  . LYS   A 1 153 ? 28.189 -15.043 18.037  1.00 41.58  ? 332 LYS   A CG  1 
ATOM   1112 C  CD  . LYS   A 1 153 ? 29.053 -14.124 18.878  1.00 44.60  ? 332 LYS   A CD  1 
ATOM   1113 C  CE  . LYS   A 1 153 ? 28.260 -13.107 19.672  1.00 46.72  ? 332 LYS   A CE  1 
ATOM   1114 N  NZ  . LYS   A 1 153 ? 29.150 -12.156 20.379  1.00 46.76  ? 332 LYS   A NZ  1 
ATOM   1115 N  N   . ASP   A 1 154 ? 32.152 -15.140 16.219  1.00 38.00  ? 333 ASP   A N   1 
ATOM   1116 C  CA  . ASP   A 1 154 ? 33.563 -15.491 16.303  1.00 38.58  ? 333 ASP   A CA  1 
ATOM   1117 C  C   . ASP   A 1 154 ? 34.004 -16.237 15.045  1.00 38.15  ? 333 ASP   A C   1 
ATOM   1118 O  O   . ASP   A 1 154 ? 34.615 -17.301 15.131  1.00 37.79  ? 333 ASP   A O   1 
ATOM   1119 C  CB  . ASP   A 1 154 ? 33.880 -16.258 17.592  1.00 40.72  ? 333 ASP   A CB  1 
ATOM   1120 C  CG  . ASP   A 1 154 ? 33.480 -15.526 18.863  1.00 42.40  ? 333 ASP   A CG  1 
ATOM   1121 O  OD1 . ASP   A 1 154 ? 33.927 -14.374 19.044  1.00 44.00  ? 333 ASP   A OD1 1 
ATOM   1122 O  OD2 . ASP   A 1 154 ? 32.734 -16.117 19.667  1.00 43.53  ? 333 ASP   A OD2 1 
ATOM   1123 N  N   . TRP   A 1 155 ? 33.690 -15.667 13.875  1.00 37.18  ? 334 TRP   A N   1 
ATOM   1124 C  CA  . TRP   A 1 155 ? 34.139 -16.240 12.617  1.00 35.70  ? 334 TRP   A CA  1 
ATOM   1125 C  C   . TRP   A 1 155 ? 35.631 -15.976 12.445  1.00 37.19  ? 334 TRP   A C   1 
ATOM   1126 O  O   . TRP   A 1 155 ? 36.089 -14.851 12.634  1.00 37.83  ? 334 TRP   A O   1 
ATOM   1127 C  CB  . TRP   A 1 155 ? 33.349 -15.677 11.431  1.00 32.63  ? 334 TRP   A CB  1 
ATOM   1128 C  CG  . TRP   A 1 155 ? 33.668 -16.368 10.140  1.00 30.18  ? 334 TRP   A CG  1 
ATOM   1129 C  CD1 . TRP   A 1 155 ? 34.611 -16.004 9.221   1.00 29.73  ? 334 TRP   A CD1 1 
ATOM   1130 C  CD2 . TRP   A 1 155 ? 33.023 -17.539 9.610   1.00 29.43  ? 334 TRP   A CD2 1 
ATOM   1131 N  NE1 . TRP   A 1 155 ? 34.608 -16.876 8.164   1.00 29.32  ? 334 TRP   A NE1 1 
ATOM   1132 C  CE2 . TRP   A 1 155 ? 33.643 -17.827 8.373   1.00 28.65  ? 334 TRP   A CE2 1 
ATOM   1133 C  CE3 . TRP   A 1 155 ? 31.994 -18.376 10.061  1.00 29.12  ? 334 TRP   A CE3 1 
ATOM   1134 C  CZ2 . TRP   A 1 155 ? 33.259 -18.912 7.585   1.00 28.57  ? 334 TRP   A CZ2 1 
ATOM   1135 C  CZ3 . TRP   A 1 155 ? 31.618 -19.448 9.282   1.00 29.29  ? 334 TRP   A CZ3 1 
ATOM   1136 C  CH2 . TRP   A 1 155 ? 32.244 -19.711 8.062   1.00 29.30  ? 334 TRP   A CH2 1 
ATOM   1137 N  N   . ASP   A 1 156 ? 36.368 -17.027 12.074  1.00 39.46  ? 335 ASP   A N   1 
ATOM   1138 C  CA  . ASP   A 1 156 ? 37.784 -16.918 11.768  1.00 41.13  ? 335 ASP   A CA  1 
ATOM   1139 C  C   . ASP   A 1 156 ? 38.039 -17.500 10.380  1.00 40.72  ? 335 ASP   A C   1 
ATOM   1140 O  O   . ASP   A 1 156 ? 38.032 -18.718 10.203  1.00 39.66  ? 335 ASP   A O   1 
ATOM   1141 C  CB  . ASP   A 1 156 ? 38.640 -17.542 12.875  1.00 43.10  ? 335 ASP   A CB  1 
ATOM   1142 C  CG  . ASP   A 1 156 ? 40.124 -17.588 12.552  1.00 44.27  ? 335 ASP   A CG  1 
ATOM   1143 O  OD1 . ASP   A 1 156 ? 40.648 -16.572 12.051  1.00 44.55  ? 335 ASP   A OD1 1 
ATOM   1144 O  OD2 . ASP   A 1 156 ? 40.746 -18.635 12.820  1.00 45.44  ? 335 ASP   A OD2 1 
ATOM   1145 N  N   . ALA   A 1 157 ? 38.272 -16.604 9.410   1.00 40.65  ? 336 ALA   A N   1 
ATOM   1146 C  CA  . ALA   A 1 157 ? 38.380 -16.954 8.002   1.00 40.48  ? 336 ALA   A CA  1 
ATOM   1147 C  C   . ALA   A 1 157 ? 39.669 -17.726 7.724   1.00 41.47  ? 336 ALA   A C   1 
ATOM   1148 O  O   . ALA   A 1 157 ? 39.760 -18.446 6.730   1.00 40.58  ? 336 ALA   A O   1 
ATOM   1149 C  CB  . ALA   A 1 157 ? 38.284 -15.711 7.153   1.00 39.26  ? 336 ALA   A CB  1 
ATOM   1150 N  N   . LYS   A 1 158 ? 40.660 -17.569 8.609   1.00 42.85  ? 337 LYS   A N   1 
ATOM   1151 C  CA  . LYS   A 1 158 ? 41.914 -18.301 8.515   1.00 43.83  ? 337 LYS   A CA  1 
ATOM   1152 C  C   . LYS   A 1 158 ? 41.648 -19.803 8.572   1.00 42.42  ? 337 LYS   A C   1 
ATOM   1153 O  O   . LYS   A 1 158 ? 42.348 -20.582 7.929   1.00 42.84  ? 337 LYS   A O   1 
ATOM   1154 C  CB  . LYS   A 1 158 ? 42.874 -17.869 9.629   1.00 45.88  ? 337 LYS   A CB  1 
ATOM   1155 C  CG  . LYS   A 1 158 ? 43.640 -16.575 9.377   1.00 48.23  ? 337 LYS   A CG  1 
ATOM   1156 C  CD  . LYS   A 1 158 ? 44.968 -16.756 8.652   1.00 50.22  ? 337 LYS   A CD  1 
ATOM   1157 C  CE  . LYS   A 1 158 ? 44.860 -17.264 7.228   1.00 51.41  ? 337 LYS   A CE  1 
ATOM   1158 N  NZ  . LYS   A 1 158 ? 44.087 -16.343 6.361   1.00 51.88  ? 337 LYS   A NZ  1 
ATOM   1159 N  N   . VAL   A 1 159 ? 40.616 -20.188 9.334   1.00 41.33  ? 338 VAL   A N   1 
ATOM   1160 C  CA  . VAL   A 1 159 ? 40.302 -21.584 9.593   1.00 39.64  ? 338 VAL   A CA  1 
ATOM   1161 C  C   . VAL   A 1 159 ? 39.045 -21.989 8.822   1.00 38.01  ? 338 VAL   A C   1 
ATOM   1162 O  O   . VAL   A 1 159 ? 38.989 -23.084 8.264   1.00 38.03  ? 338 VAL   A O   1 
ATOM   1163 C  CB  . VAL   A 1 159 ? 40.171 -21.851 11.108  1.00 40.56  ? 338 VAL   A CB  1 
ATOM   1164 C  CG1 . VAL   A 1 159 ? 39.625 -23.239 11.412  1.00 41.01  ? 338 VAL   A CG1 1 
ATOM   1165 C  CG2 . VAL   A 1 159 ? 41.492 -21.633 11.832  1.00 41.29  ? 338 VAL   A CG2 1 
ATOM   1166 N  N   . SER   A 1 160 ? 38.049 -21.094 8.782   1.00 35.37  ? 339 SER   A N   1 
ATOM   1167 C  CA  . SER   A 1 160 ? 36.722 -21.439 8.293   1.00 33.14  ? 339 SER   A CA  1 
ATOM   1168 C  C   . SER   A 1 160 ? 36.503 -20.945 6.864   1.00 32.02  ? 339 SER   A C   1 
ATOM   1169 O  O   . SER   A 1 160 ? 35.569 -21.390 6.197   1.00 31.55  ? 339 SER   A O   1 
ATOM   1170 C  CB  . SER   A 1 160 ? 35.653 -20.923 9.222   1.00 32.99  ? 339 SER   A CB  1 
ATOM   1171 O  OG  . SER   A 1 160 ? 35.807 -21.466 10.525  1.00 32.22  ? 339 SER   A OG  1 
ATOM   1172 N  N   . GLY   A 1 161 ? 37.361 -20.022 6.409   1.00 29.54  ? 340 GLY   A N   1 
ATOM   1173 C  CA  . GLY   A 1 161 ? 37.244 -19.429 5.085   1.00 29.14  ? 340 GLY   A CA  1 
ATOM   1174 C  C   . GLY   A 1 161 ? 35.976 -18.588 4.942   1.00 27.17  ? 340 GLY   A C   1 
ATOM   1175 O  O   . GLY   A 1 161 ? 35.653 -17.794 5.821   1.00 27.61  ? 340 GLY   A O   1 
ATOM   1176 N  N   . GLY   A 1 162 ? 35.270 -18.775 3.822   1.00 26.87  ? 341 GLY   A N   1 
ATOM   1177 C  CA  . GLY   A 1 162 ? 33.958 -18.184 3.606   1.00 26.05  ? 341 GLY   A CA  1 
ATOM   1178 C  C   . GLY   A 1 162 ? 34.016 -16.685 3.319   1.00 25.63  ? 341 GLY   A C   1 
ATOM   1179 O  O   . GLY   A 1 162 ? 33.022 -15.981 3.492   1.00 25.76  ? 341 GLY   A O   1 
ATOM   1180 N  N   . ILE   A 1 163 ? 35.184 -16.208 2.870   1.00 25.35  ? 342 ILE   A N   1 
ATOM   1181 C  CA  . ILE   A 1 163 ? 35.362 -14.803 2.537   1.00 25.83  ? 342 ILE   A CA  1 
ATOM   1182 C  C   . ILE   A 1 163 ? 34.529 -14.467 1.300   1.00 24.93  ? 342 ILE   A C   1 
ATOM   1183 O  O   . ILE   A 1 163 ? 34.515 -15.218 0.328   1.00 24.47  ? 342 ILE   A O   1 
ATOM   1184 C  CB  . ILE   A 1 163 ? 36.859 -14.478 2.351   1.00 26.98  ? 342 ILE   A CB  1 
ATOM   1185 C  CG1 . ILE   A 1 163 ? 37.602 -14.498 3.690   1.00 28.05  ? 342 ILE   A CG1 1 
ATOM   1186 C  CG2 . ILE   A 1 163 ? 37.054 -13.151 1.629   1.00 27.11  ? 342 ILE   A CG2 1 
ATOM   1187 C  CD1 . ILE   A 1 163 ? 39.105 -14.343 3.575   1.00 29.75  ? 342 ILE   A CD1 1 
ATOM   1188 N  N   . LEU   A 1 164 ? 33.812 -13.339 1.359   1.00 24.46  ? 343 LEU   A N   1 
ATOM   1189 C  CA  . LEU   A 1 164 ? 33.250 -12.753 0.154   1.00 24.03  ? 343 LEU   A CA  1 
ATOM   1190 C  C   . LEU   A 1 164 ? 34.325 -11.887 -0.491  1.00 23.84  ? 343 LEU   A C   1 
ATOM   1191 O  O   . LEU   A 1 164 ? 34.794 -10.920 0.108   1.00 23.93  ? 343 LEU   A O   1 
ATOM   1192 C  CB  . LEU   A 1 164 ? 31.996 -11.936 0.485   1.00 24.00  ? 343 LEU   A CB  1 
ATOM   1193 C  CG  . LEU   A 1 164 ? 31.464 -11.065 -0.656  1.00 24.64  ? 343 LEU   A CG  1 
ATOM   1194 C  CD1 . LEU   A 1 164 ? 30.968 -11.915 -1.818  1.00 25.35  ? 343 LEU   A CD1 1 
ATOM   1195 C  CD2 . LEU   A 1 164 ? 30.352 -10.153 -0.170  1.00 25.09  ? 343 LEU   A CD2 1 
ATOM   1196 N  N   . ARG   A 1 165 ? 34.719 -12.269 -1.708  1.00 24.03  ? 344 ARG   A N   1 
ATOM   1197 C  CA  . ARG   A 1 165 ? 35.691 -11.506 -2.470  1.00 23.47  ? 344 ARG   A CA  1 
ATOM   1198 C  C   . ARG   A 1 165 ? 34.954 -10.761 -3.575  1.00 23.09  ? 344 ARG   A C   1 
ATOM   1199 O  O   . ARG   A 1 165 ? 34.237 -11.372 -4.363  1.00 23.12  ? 344 ARG   A O   1 
ATOM   1200 C  CB  . ARG   A 1 165 ? 36.780 -12.426 -3.032  1.00 23.82  ? 344 ARG   A CB  1 
ATOM   1201 C  CG  . ARG   A 1 165 ? 37.857 -11.694 -3.821  1.00 24.35  ? 344 ARG   A CG  1 
ATOM   1202 C  CD  . ARG   A 1 165 ? 39.096 -12.550 -3.993  1.00 25.27  ? 344 ARG   A CD  1 
ATOM   1203 N  NE  . ARG   A 1 165 ? 39.815 -12.693 -2.736  1.00 26.73  ? 344 ARG   A NE  1 
ATOM   1204 C  CZ  . ARG   A 1 165 ? 40.736 -13.617 -2.492  1.00 27.32  ? 344 ARG   A CZ  1 
ATOM   1205 N  NH1 . ARG   A 1 165 ? 40.997 -14.541 -3.398  1.00 28.43  ? 344 ARG   A NH1 1 
ATOM   1206 N  NH2 . ARG   A 1 165 ? 41.370 -13.631 -1.332  1.00 27.10  ? 344 ARG   A NH2 1 
ATOM   1207 N  N   . ILE   A 1 166 ? 35.129 -9.435  -3.606  1.00 23.24  ? 345 ILE   A N   1 
ATOM   1208 C  CA  . ILE   A 1 166 ? 34.480 -8.603  -4.606  1.00 23.38  ? 345 ILE   A CA  1 
ATOM   1209 C  C   . ILE   A 1 166 ? 35.565 -8.033  -5.514  1.00 24.13  ? 345 ILE   A C   1 
ATOM   1210 O  O   . ILE   A 1 166 ? 36.571 -7.521  -5.031  1.00 24.32  ? 345 ILE   A O   1 
ATOM   1211 C  CB  . ILE   A 1 166 ? 33.632 -7.482  -3.966  1.00 23.03  ? 345 ILE   A CB  1 
ATOM   1212 C  CG1 . ILE   A 1 166 ? 32.725 -7.992  -2.840  1.00 23.18  ? 345 ILE   A CG1 1 
ATOM   1213 C  CG2 . ILE   A 1 166 ? 32.841 -6.734  -5.034  1.00 22.57  ? 345 ILE   A CG2 1 
ATOM   1214 C  CD1 . ILE   A 1 166 ? 31.946 -6.896  -2.128  1.00 23.87  ? 345 ILE   A CD1 1 
ATOM   1215 N  N   . PHE   A 1 167 ? 35.331 -8.126  -6.827  1.00 25.12  ? 346 PHE   A N   1 
ATOM   1216 C  CA  . PHE   A 1 167 ? 36.253 -7.610  -7.824  1.00 26.44  ? 346 PHE   A CA  1 
ATOM   1217 C  C   . PHE   A 1 167 ? 35.593 -6.447  -8.563  1.00 26.08  ? 346 PHE   A C   1 
ATOM   1218 O  O   . PHE   A 1 167 ? 35.067 -6.636  -9.659  1.00 25.28  ? 346 PHE   A O   1 
ATOM   1219 C  CB  . PHE   A 1 167 ? 36.629 -8.698  -8.834  1.00 27.51  ? 346 PHE   A CB  1 
ATOM   1220 C  CG  . PHE   A 1 167 ? 37.013 -10.041 -8.262  1.00 29.21  ? 346 PHE   A CG  1 
ATOM   1221 C  CD1 . PHE   A 1 167 ? 36.044 -10.981 -7.941  1.00 29.94  ? 346 PHE   A CD1 1 
ATOM   1222 C  CD2 . PHE   A 1 167 ? 38.345 -10.370 -8.055  1.00 29.83  ? 346 PHE   A CD2 1 
ATOM   1223 C  CE1 . PHE   A 1 167 ? 36.400 -12.221 -7.429  1.00 30.53  ? 346 PHE   A CE1 1 
ATOM   1224 C  CE2 . PHE   A 1 167 ? 38.699 -11.609 -7.538  1.00 29.41  ? 346 PHE   A CE2 1 
ATOM   1225 C  CZ  . PHE   A 1 167 ? 37.727 -12.533 -7.233  1.00 28.92  ? 346 PHE   A CZ  1 
ATOM   1226 N  N   . PRO   A 1 168 ? 35.602 -5.214  -8.003  1.00 26.46  ? 347 PRO   A N   1 
ATOM   1227 C  CA  . PRO   A 1 168 ? 34.976 -4.070  -8.668  1.00 26.68  ? 347 PRO   A CA  1 
ATOM   1228 C  C   . PRO   A 1 168 ? 35.543 -3.869  -10.072 1.00 26.50  ? 347 PRO   A C   1 
ATOM   1229 O  O   . PRO   A 1 168 ? 36.753 -3.944  -10.278 1.00 25.33  ? 347 PRO   A O   1 
ATOM   1230 C  CB  . PRO   A 1 168 ? 35.245 -2.872  -7.744  1.00 27.28  ? 347 PRO   A CB  1 
ATOM   1231 C  CG  . PRO   A 1 168 ? 36.316 -3.344  -6.775  1.00 26.92  ? 347 PRO   A CG  1 
ATOM   1232 C  CD  . PRO   A 1 168 ? 36.203 -4.851  -6.710  1.00 26.25  ? 347 PRO   A CD  1 
ATOM   1233 N  N   . GLU   A 1 169 ? 34.635 -3.648  -11.031 1.00 26.89  ? 348 GLU   A N   1 
ATOM   1234 C  CA  . GLU   A 1 169 ? 34.961 -3.586  -12.445 1.00 27.66  ? 348 GLU   A CA  1 
ATOM   1235 C  C   . GLU   A 1 169 ? 35.913 -2.421  -12.701 1.00 26.76  ? 348 GLU   A C   1 
ATOM   1236 O  O   . GLU   A 1 169 ? 35.628 -1.287  -12.327 1.00 26.33  ? 348 GLU   A O   1 
ATOM   1237 C  CB  . GLU   A 1 169 ? 33.684 -3.436  -13.275 1.00 29.01  ? 348 GLU   A CB  1 
ATOM   1238 C  CG  . GLU   A 1 169 ? 33.927 -3.384  -14.775 1.00 30.29  ? 348 GLU   A CG  1 
ATOM   1239 C  CD  . GLU   A 1 169 ? 32.680 -3.177  -15.620 1.00 32.74  ? 348 GLU   A CD  1 
ATOM   1240 O  OE1 . GLU   A 1 169 ? 31.604 -2.934  -15.041 1.00 33.60  ? 348 GLU   A OE1 1 
ATOM   1241 O  OE2 . GLU   A 1 169 ? 32.788 -3.261  -16.860 1.00 33.92  ? 348 GLU   A OE2 1 
ATOM   1242 N  N   . GLY   A 1 170 ? 37.047 -2.732  -13.337 1.00 26.67  ? 349 GLY   A N   1 
ATOM   1243 C  CA  . GLY   A 1 170 ? 37.982 -1.725  -13.811 1.00 27.14  ? 349 GLY   A CA  1 
ATOM   1244 C  C   . GLY   A 1 170 ? 38.700 -1.006  -12.673 1.00 27.03  ? 349 GLY   A C   1 
ATOM   1245 O  O   . GLY   A 1 170 ? 39.061 0.158   -12.815 1.00 27.74  ? 349 GLY   A O   1 
ATOM   1246 N  N   . LYS   A 1 171 ? 38.892 -1.708  -11.549 1.00 26.19  ? 350 LYS   A N   1 
ATOM   1247 C  CA  . LYS   A 1 171 ? 39.674 -1.175  -10.444 1.00 26.51  ? 350 LYS   A CA  1 
ATOM   1248 C  C   . LYS   A 1 171 ? 40.896 -2.060  -10.209 1.00 25.70  ? 350 LYS   A C   1 
ATOM   1249 O  O   . LYS   A 1 171 ? 40.843 -3.265  -10.442 1.00 25.96  ? 350 LYS   A O   1 
ATOM   1250 C  CB  . LYS   A 1 171 ? 38.803 -0.994  -9.196  1.00 27.88  ? 350 LYS   A CB  1 
ATOM   1251 C  CG  . LYS   A 1 171 ? 37.559 -0.144  -9.427  1.00 29.93  ? 350 LYS   A CG  1 
ATOM   1252 C  CD  . LYS   A 1 171 ? 37.023 0.530   -8.195  1.00 31.49  ? 350 LYS   A CD  1 
ATOM   1253 C  CE  . LYS   A 1 171 ? 35.963 1.558   -8.532  1.00 33.13  ? 350 LYS   A CE  1 
ATOM   1254 N  NZ  . LYS   A 1 171 ? 35.603 2.373   -7.349  1.00 35.89  ? 350 LYS   A NZ  1 
ATOM   1255 N  N   . ALA   A 1 172 ? 41.990 -1.439  -9.750  1.00 24.56  ? 351 ALA   A N   1 
ATOM   1256 C  CA  . ALA   A 1 172 ? 43.256 -2.120  -9.523  1.00 24.46  ? 351 ALA   A CA  1 
ATOM   1257 C  C   . ALA   A 1 172 ? 43.266 -2.806  -8.157  1.00 24.41  ? 351 ALA   A C   1 
ATOM   1258 O  O   . ALA   A 1 172 ? 44.306 -3.296  -7.721  1.00 23.91  ? 351 ALA   A O   1 
ATOM   1259 C  CB  . ALA   A 1 172 ? 44.399 -1.137  -9.650  1.00 23.57  ? 351 ALA   A CB  1 
ATOM   1260 N  N   . GLN   A 1 173 ? 42.105 -2.832  -7.489  1.00 25.15  ? 352 GLN   A N   1 
ATOM   1261 C  CA  . GLN   A 1 173 ? 41.973 -3.444  -6.178  1.00 26.40  ? 352 GLN   A CA  1 
ATOM   1262 C  C   . GLN   A 1 173 ? 40.754 -4.363  -6.138  1.00 25.56  ? 352 GLN   A C   1 
ATOM   1263 O  O   . GLN   A 1 173 ? 39.806 -4.190  -6.900  1.00 26.20  ? 352 GLN   A O   1 
ATOM   1264 C  CB  . GLN   A 1 173 ? 41.826 -2.376  -5.094  1.00 30.15  ? 352 GLN   A CB  1 
ATOM   1265 C  CG  . GLN   A 1 173 ? 43.138 -1.732  -4.667  1.00 34.84  ? 352 GLN   A CG  1 
ATOM   1266 C  CD  . GLN   A 1 173 ? 42.992 -0.984  -3.363  1.00 38.68  ? 352 GLN   A CD  1 
ATOM   1267 O  OE1 . GLN   A 1 173 ? 43.588 -1.340  -2.347  1.00 40.82  ? 352 GLN   A OE1 1 
ATOM   1268 N  NE2 . GLN   A 1 173 ? 42.177 0.058   -3.376  1.00 40.32  ? 352 GLN   A NE2 1 
ATOM   1269 N  N   . PHE   A 1 174 ? 40.795 -5.337  -5.224  1.00 23.67  ? 353 PHE   A N   1 
ATOM   1270 C  CA  . PHE   A 1 174 ? 39.637 -6.152  -4.891  1.00 23.50  ? 353 PHE   A CA  1 
ATOM   1271 C  C   . PHE   A 1 174 ? 39.426 -6.090  -3.380  1.00 23.08  ? 353 PHE   A C   1 
ATOM   1272 O  O   . PHE   A 1 174 ? 40.323 -5.678  -2.647  1.00 22.59  ? 353 PHE   A O   1 
ATOM   1273 C  CB  . PHE   A 1 174 ? 39.820 -7.594  -5.372  1.00 23.44  ? 353 PHE   A CB  1 
ATOM   1274 C  CG  . PHE   A 1 174 ? 40.980 -8.325  -4.741  1.00 24.31  ? 353 PHE   A CG  1 
ATOM   1275 C  CD1 . PHE   A 1 174 ? 42.276 -8.134  -5.201  1.00 24.74  ? 353 PHE   A CD1 1 
ATOM   1276 C  CD2 . PHE   A 1 174 ? 40.781 -9.179  -3.666  1.00 24.57  ? 353 PHE   A CD2 1 
ATOM   1277 C  CE1 . PHE   A 1 174 ? 43.345 -8.794  -4.612  1.00 25.08  ? 353 PHE   A CE1 1 
ATOM   1278 C  CE2 . PHE   A 1 174 ? 41.852 -9.838  -3.078  1.00 24.85  ? 353 PHE   A CE2 1 
ATOM   1279 C  CZ  . PHE   A 1 174 ? 43.128 -9.647  -3.553  1.00 24.59  ? 353 PHE   A CZ  1 
ATOM   1280 N  N   . ALA   A 1 175 ? 38.238 -6.511  -2.930  1.00 23.34  ? 354 ALA   A N   1 
ATOM   1281 C  CA  . ALA   A 1 175 ? 37.868 -6.416  -1.526  1.00 24.04  ? 354 ALA   A CA  1 
ATOM   1282 C  C   . ALA   A 1 175 ? 37.600 -7.807  -0.959  1.00 23.71  ? 354 ALA   A C   1 
ATOM   1283 O  O   . ALA   A 1 175 ? 36.869 -8.590  -1.559  1.00 24.23  ? 354 ALA   A O   1 
ATOM   1284 C  CB  . ALA   A 1 175 ? 36.661 -5.516  -1.377  1.00 23.42  ? 354 ALA   A CB  1 
ATOM   1285 N  N   . ASP   A 1 176 ? 38.198 -8.096  0.204   1.00 24.57  ? 355 ASP   A N   1 
ATOM   1286 C  CA  . ASP   A 1 176 ? 37.930 -9.323  0.937   1.00 25.76  ? 355 ASP   A CA  1 
ATOM   1287 C  C   . ASP   A 1 176 ? 37.070 -8.995  2.155   1.00 26.12  ? 355 ASP   A C   1 
ATOM   1288 O  O   . ASP   A 1 176 ? 37.519 -8.287  3.056   1.00 26.44  ? 355 ASP   A O   1 
ATOM   1289 C  CB  . ASP   A 1 176 ? 39.223 -10.050 1.327   1.00 26.25  ? 355 ASP   A CB  1 
ATOM   1290 C  CG  . ASP   A 1 176 ? 39.883 -10.800 0.182   1.00 27.24  ? 355 ASP   A CG  1 
ATOM   1291 O  OD1 . ASP   A 1 176 ? 39.381 -10.702 -0.957  1.00 26.98  ? 355 ASP   A OD1 1 
ATOM   1292 O  OD2 . ASP   A 1 176 ? 40.892 -11.485 0.438   1.00 27.44  ? 355 ASP   A OD2 1 
ATOM   1293 N  N   . ILE   A 1 177 ? 35.832 -9.506  2.164   1.00 25.39  ? 356 ILE   A N   1 
ATOM   1294 C  CA  . ILE   A 1 177 ? 34.916 -9.257  3.267   1.00 25.78  ? 356 ILE   A CA  1 
ATOM   1295 C  C   . ILE   A 1 177 ? 34.718 -10.557 4.043   1.00 25.94  ? 356 ILE   A C   1 
ATOM   1296 O  O   . ILE   A 1 177 ? 34.130 -11.509 3.529   1.00 25.58  ? 356 ILE   A O   1 
ATOM   1297 C  CB  . ILE   A 1 177 ? 33.565 -8.690  2.774   1.00 26.06  ? 356 ILE   A CB  1 
ATOM   1298 C  CG1 . ILE   A 1 177 ? 33.711 -7.663  1.645   1.00 26.55  ? 356 ILE   A CG1 1 
ATOM   1299 C  CG2 . ILE   A 1 177 ? 32.736 -8.156  3.939   1.00 26.64  ? 356 ILE   A CG2 1 
ATOM   1300 C  CD1 . ILE   A 1 177 ? 34.467 -6.408  2.018   1.00 27.32  ? 356 ILE   A CD1 1 
ATOM   1301 N  N   . GLU   A 1 178 ? 35.195 -10.574 5.291   1.00 26.12  ? 357 GLU   A N   1 
ATOM   1302 C  CA  . GLU   A 1 178 ? 34.932 -11.692 6.182   1.00 28.14  ? 357 GLU   A CA  1 
ATOM   1303 C  C   . GLU   A 1 178 ? 33.480 -11.614 6.641   1.00 26.38  ? 357 GLU   A C   1 
ATOM   1304 O  O   . GLU   A 1 178 ? 32.982 -10.522 6.909   1.00 25.76  ? 357 GLU   A O   1 
ATOM   1305 C  CB  . GLU   A 1 178 ? 35.901 -11.694 7.366   1.00 29.94  ? 357 GLU   A CB  1 
ATOM   1306 C  CG  . GLU   A 1 178 ? 37.352 -11.848 6.947   1.00 33.77  ? 357 GLU   A CG  1 
ATOM   1307 C  CD  . GLU   A 1 178 ? 38.360 -11.735 8.078   1.00 37.91  ? 357 GLU   A CD  1 
ATOM   1308 O  OE1 . GLU   A 1 178 ? 39.228 -12.624 8.189   1.00 39.03  ? 357 GLU   A OE1 1 
ATOM   1309 O  OE2 . GLU   A 1 178 ? 38.275 -10.756 8.847   1.00 41.82  ? 357 GLU   A OE2 1 
ATOM   1310 N  N   . PRO   A 1 179 ? 32.761 -12.759 6.730   1.00 26.07  ? 358 PRO   A N   1 
ATOM   1311 C  CA  . PRO   A 1 179 ? 31.352 -12.762 7.129   1.00 25.81  ? 358 PRO   A CA  1 
ATOM   1312 C  C   . PRO   A 1 179 ? 31.188 -12.624 8.643   1.00 26.83  ? 358 PRO   A C   1 
ATOM   1313 O  O   . PRO   A 1 179 ? 30.580 -13.478 9.289   1.00 25.27  ? 358 PRO   A O   1 
ATOM   1314 C  CB  . PRO   A 1 179 ? 30.858 -14.122 6.608   1.00 24.98  ? 358 PRO   A CB  1 
ATOM   1315 C  CG  . PRO   A 1 179 ? 32.078 -15.021 6.682   1.00 25.37  ? 358 PRO   A CG  1 
ATOM   1316 C  CD  . PRO   A 1 179 ? 33.269 -14.113 6.446   1.00 25.58  ? 358 PRO   A CD  1 
ATOM   1317 N  N   . LYS   A 1 180 ? 31.712 -11.509 9.177   1.00 28.51  ? 359 LYS   A N   1 
ATOM   1318 C  CA  . LYS   A 1 180 ? 31.856 -11.255 10.604  1.00 29.46  ? 359 LYS   A CA  1 
ATOM   1319 C  C   . LYS   A 1 180 ? 30.504 -10.982 11.261  1.00 27.94  ? 359 LYS   A C   1 
ATOM   1320 O  O   . LYS   A 1 180 ? 29.634 -10.343 10.676  1.00 26.14  ? 359 LYS   A O   1 
ATOM   1321 C  CB  . LYS   A 1 180 ? 32.744 -10.026 10.833  1.00 32.72  ? 359 LYS   A CB  1 
ATOM   1322 C  CG  . LYS   A 1 180 ? 34.201 -10.304 11.177  1.00 38.75  ? 359 LYS   A CG  1 
ATOM   1323 C  CD  . LYS   A 1 180 ? 35.043 -9.040  11.303  1.00 40.88  ? 359 LYS   A CD  1 
ATOM   1324 C  CE  . LYS   A 1 180 ? 34.460 -7.985  12.223  1.00 42.19  ? 359 LYS   A CE  1 
ATOM   1325 N  NZ  . LYS   A 1 180 ? 34.559 -8.369  13.651  1.00 43.59  ? 359 LYS   A NZ  1 
ATOM   1326 N  N   . PHE   A 1 181 ? 30.373 -11.427 12.515  1.00 27.44  ? 360 PHE   A N   1 
ATOM   1327 C  CA  . PHE   A 1 181 ? 29.205 -11.151 13.338  1.00 27.50  ? 360 PHE   A CA  1 
ATOM   1328 C  C   . PHE   A 1 181 ? 28.882 -9.658  13.315  1.00 26.62  ? 360 PHE   A C   1 
ATOM   1329 O  O   . PHE   A 1 181 ? 29.763 -8.827  13.539  1.00 25.99  ? 360 PHE   A O   1 
ATOM   1330 C  CB  . PHE   A 1 181 ? 29.457 -11.613 14.776  1.00 28.17  ? 360 PHE   A CB  1 
ATOM   1331 C  CG  . PHE   A 1 181 ? 28.331 -11.341 15.741  1.00 28.88  ? 360 PHE   A CG  1 
ATOM   1332 C  CD1 . PHE   A 1 181 ? 27.203 -12.149 15.768  1.00 29.63  ? 360 PHE   A CD1 1 
ATOM   1333 C  CD2 . PHE   A 1 181 ? 28.397 -10.268 16.619  1.00 29.74  ? 360 PHE   A CD2 1 
ATOM   1334 C  CE1 . PHE   A 1 181 ? 26.170 -11.896 16.660  1.00 30.12  ? 360 PHE   A CE1 1 
ATOM   1335 C  CE2 . PHE   A 1 181 ? 27.363 -10.014 17.508  1.00 29.38  ? 360 PHE   A CE2 1 
ATOM   1336 C  CZ  . PHE   A 1 181 ? 26.254 -10.830 17.529  1.00 30.32  ? 360 PHE   A CZ  1 
ATOM   1337 N  N   . ASP   A 1 182 ? 27.611 -9.346  13.021  1.00 25.50  ? 361 ASP   A N   1 
ATOM   1338 C  CA  . ASP   A 1 182 ? 27.027 -8.014  13.140  1.00 25.82  ? 361 ASP   A CA  1 
ATOM   1339 C  C   . ASP   A 1 182 ? 27.623 -7.042  12.118  1.00 25.39  ? 361 ASP   A C   1 
ATOM   1340 O  O   . ASP   A 1 182 ? 27.608 -5.828  12.323  1.00 24.62  ? 361 ASP   A O   1 
ATOM   1341 C  CB  . ASP   A 1 182 ? 27.060 -7.516  14.591  1.00 26.33  ? 361 ASP   A CB  1 
ATOM   1342 C  CG  . ASP   A 1 182 ? 26.197 -6.290  14.849  1.00 27.33  ? 361 ASP   A CG  1 
ATOM   1343 O  OD1 . ASP   A 1 182 ? 25.075 -6.232  14.306  1.00 26.56  ? 361 ASP   A OD1 1 
ATOM   1344 O  OD2 . ASP   A 1 182 ? 26.641 -5.417  15.622  1.00 28.11  ? 361 ASP   A OD2 1 
ATOM   1345 N  N   . ARG   A 1 183 ? 28.117 -7.585  10.999  1.00 24.71  ? 362 ARG   A N   1 
ATOM   1346 C  CA  . ARG   A 1 183 ? 28.657 -6.782  9.913   1.00 23.54  ? 362 ARG   A CA  1 
ATOM   1347 C  C   . ARG   A 1 183 ? 27.587 -6.565  8.843   1.00 23.17  ? 362 ARG   A C   1 
ATOM   1348 O  O   . ARG   A 1 183 ? 26.909 -7.504  8.435   1.00 23.71  ? 362 ARG   A O   1 
ATOM   1349 C  CB  . ARG   A 1 183 ? 29.900 -7.462  9.327   1.00 22.92  ? 362 ARG   A CB  1 
ATOM   1350 C  CG  . ARG   A 1 183 ? 30.391 -6.858  8.019   1.00 23.11  ? 362 ARG   A CG  1 
ATOM   1351 C  CD  . ARG   A 1 183 ? 31.736 -7.415  7.592   1.00 24.05  ? 362 ARG   A CD  1 
ATOM   1352 N  NE  . ARG   A 1 183 ? 32.809 -6.826  8.384   1.00 24.04  ? 362 ARG   A NE  1 
ATOM   1353 C  CZ  . ARG   A 1 183 ? 34.099 -7.119  8.266   1.00 25.02  ? 362 ARG   A CZ  1 
ATOM   1354 N  NH1 . ARG   A 1 183 ? 34.987 -6.466  8.995   1.00 25.44  ? 362 ARG   A NH1 1 
ATOM   1355 N  NH2 . ARG   A 1 183 ? 34.503 -8.048  7.413   1.00 24.20  ? 362 ARG   A NH2 1 
ATOM   1356 N  N   . LEU   A 1 184 ? 27.465 -5.314  8.384   1.00 22.99  ? 363 LEU   A N   1 
ATOM   1357 C  CA  . LEU   A 1 184 ? 26.567 -4.953  7.298   1.00 23.41  ? 363 LEU   A CA  1 
ATOM   1358 C  C   . LEU   A 1 184 ? 27.399 -4.535  6.087   1.00 23.91  ? 363 LEU   A C   1 
ATOM   1359 O  O   . LEU   A 1 184 ? 28.413 -3.853  6.237   1.00 25.15  ? 363 LEU   A O   1 
ATOM   1360 C  CB  . LEU   A 1 184 ? 25.666 -3.807  7.775   1.00 23.36  ? 363 LEU   A CB  1 
ATOM   1361 C  CG  . LEU   A 1 184 ? 24.540 -3.391  6.830   1.00 23.60  ? 363 LEU   A CG  1 
ATOM   1362 C  CD1 . LEU   A 1 184 ? 23.431 -4.436  6.816   1.00 23.62  ? 363 LEU   A CD1 1 
ATOM   1363 C  CD2 . LEU   A 1 184 ? 23.981 -2.034  7.233   1.00 23.23  ? 363 LEU   A CD2 1 
ATOM   1364 N  N   . LEU   A 1 185 ? 26.957 -4.946  4.892   1.00 23.71  ? 364 LEU   A N   1 
ATOM   1365 C  CA  . LEU   A 1 185 ? 27.681 -4.679  3.658   1.00 23.99  ? 364 LEU   A CA  1 
ATOM   1366 C  C   . LEU   A 1 185 ? 26.720 -4.164  2.589   1.00 24.90  ? 364 LEU   A C   1 
ATOM   1367 O  O   . LEU   A 1 185 ? 25.631 -4.711  2.424   1.00 24.93  ? 364 LEU   A O   1 
ATOM   1368 C  CB  . LEU   A 1 185 ? 28.373 -5.971  3.204   1.00 24.13  ? 364 LEU   A CB  1 
ATOM   1369 C  CG  . LEU   A 1 185 ? 28.996 -5.954  1.806   1.00 24.37  ? 364 LEU   A CG  1 
ATOM   1370 C  CD1 . LEU   A 1 185 ? 30.242 -5.081  1.765   1.00 24.41  ? 364 LEU   A CD1 1 
ATOM   1371 C  CD2 . LEU   A 1 185 ? 29.337 -7.362  1.351   1.00 23.78  ? 364 LEU   A CD2 1 
ATOM   1372 N  N   . PHE   A 1 186 ? 27.152 -3.116  1.870   1.00 24.12  ? 365 PHE   A N   1 
ATOM   1373 C  CA  . PHE   A 1 186 ? 26.469 -2.612  0.686   1.00 25.07  ? 365 PHE   A CA  1 
ATOM   1374 C  C   . PHE   A 1 186 ? 27.414 -2.653  -0.512  1.00 24.97  ? 365 PHE   A C   1 
ATOM   1375 O  O   . PHE   A 1 186 ? 28.601 -2.367  -0.370  1.00 24.03  ? 365 PHE   A O   1 
ATOM   1376 C  CB  . PHE   A 1 186 ? 26.086 -1.137  0.843   1.00 25.99  ? 365 PHE   A CB  1 
ATOM   1377 C  CG  . PHE   A 1 186 ? 25.187 -0.799  2.004   1.00 26.93  ? 365 PHE   A CG  1 
ATOM   1378 C  CD1 . PHE   A 1 186 ? 25.708 -0.595  3.273   1.00 28.06  ? 365 PHE   A CD1 1 
ATOM   1379 C  CD2 . PHE   A 1 186 ? 23.817 -0.678  1.826   1.00 27.83  ? 365 PHE   A CD2 1 
ATOM   1380 C  CE1 . PHE   A 1 186 ? 24.878 -0.272  4.337   1.00 28.76  ? 365 PHE   A CE1 1 
ATOM   1381 C  CE2 . PHE   A 1 186 ? 22.989 -0.354  2.889   1.00 28.51  ? 365 PHE   A CE2 1 
ATOM   1382 C  CZ  . PHE   A 1 186 ? 23.520 -0.155  4.144   1.00 28.25  ? 365 PHE   A CZ  1 
ATOM   1383 N  N   . PHE   A 1 187 ? 26.863 -2.975  -1.693  1.00 25.47  ? 366 PHE   A N   1 
ATOM   1384 C  CA  . PHE   A 1 187 ? 27.581 -2.834  -2.953  1.00 25.09  ? 366 PHE   A CA  1 
ATOM   1385 C  C   . PHE   A 1 187 ? 26.592 -2.725  -4.114  1.00 25.39  ? 366 PHE   A C   1 
ATOM   1386 O  O   . PHE   A 1 187 ? 25.456 -3.185  -4.001  1.00 25.76  ? 366 PHE   A O   1 
ATOM   1387 C  CB  . PHE   A 1 187 ? 28.627 -3.945  -3.114  1.00 25.43  ? 366 PHE   A CB  1 
ATOM   1388 C  CG  . PHE   A 1 187 ? 28.098 -5.358  -3.144  1.00 25.28  ? 366 PHE   A CG  1 
ATOM   1389 C  CD1 . PHE   A 1 187 ? 27.620 -5.919  -4.321  1.00 25.51  ? 366 PHE   A CD1 1 
ATOM   1390 C  CD2 . PHE   A 1 187 ? 28.087 -6.134  -1.995  1.00 24.57  ? 366 PHE   A CD2 1 
ATOM   1391 C  CE1 . PHE   A 1 187 ? 27.141 -7.221  -4.349  1.00 25.43  ? 366 PHE   A CE1 1 
ATOM   1392 C  CE2 . PHE   A 1 187 ? 27.600 -7.433  -2.020  1.00 24.95  ? 366 PHE   A CE2 1 
ATOM   1393 C  CZ  . PHE   A 1 187 ? 27.135 -7.978  -3.198  1.00 25.42  ? 366 PHE   A CZ  1 
ATOM   1394 N  N   . TRP   A 1 188 ? 27.022 -2.089  -5.217  1.00 24.89  ? 367 TRP   A N   1 
ATOM   1395 C  CA  . TRP   A 1 188 ? 26.210 -2.024  -6.425  1.00 25.40  ? 367 TRP   A CA  1 
ATOM   1396 C  C   . TRP   A 1 188 ? 25.925 -3.444  -6.908  1.00 25.55  ? 367 TRP   A C   1 
ATOM   1397 O  O   . TRP   A 1 188 ? 26.839 -4.265  -6.977  1.00 25.44  ? 367 TRP   A O   1 
ATOM   1398 C  CB  . TRP   A 1 188 ? 26.884 -1.213  -7.544  1.00 25.54  ? 367 TRP   A CB  1 
ATOM   1399 C  CG  . TRP   A 1 188 ? 27.296 0.193   -7.225  1.00 25.35  ? 367 TRP   A CG  1 
ATOM   1400 C  CD1 . TRP   A 1 188 ? 28.531 0.736   -7.432  1.00 24.91  ? 367 TRP   A CD1 1 
ATOM   1401 C  CD2 . TRP   A 1 188 ? 26.479 1.252   -6.692  1.00 25.49  ? 367 TRP   A CD2 1 
ATOM   1402 N  NE1 . TRP   A 1 188 ? 28.545 2.051   -7.054  1.00 25.03  ? 367 TRP   A NE1 1 
ATOM   1403 C  CE2 . TRP   A 1 188 ? 27.302 2.397   -6.594  1.00 25.69  ? 367 TRP   A CE2 1 
ATOM   1404 C  CE3 . TRP   A 1 188 ? 25.145 1.347   -6.275  1.00 26.37  ? 367 TRP   A CE3 1 
ATOM   1405 C  CZ2 . TRP   A 1 188 ? 26.833 3.613   -6.098  1.00 26.17  ? 367 TRP   A CZ2 1 
ATOM   1406 C  CZ3 . TRP   A 1 188 ? 24.682 2.550   -5.787  1.00 27.09  ? 367 TRP   A CZ3 1 
ATOM   1407 C  CH2 . TRP   A 1 188 ? 25.516 3.667   -5.703  1.00 26.80  ? 367 TRP   A CH2 1 
ATOM   1408 N  N   . SER   A 1 189 ? 24.660 -3.700  -7.269  1.00 25.29  ? 368 SER   A N   1 
ATOM   1409 C  CA  . SER   A 1 189 ? 24.186 -5.026  -7.640  1.00 25.49  ? 368 SER   A CA  1 
ATOM   1410 C  C   . SER   A 1 189 ? 24.569 -5.388  -9.073  1.00 25.36  ? 368 SER   A C   1 
ATOM   1411 O  O   . SER   A 1 189 ? 24.532 -6.563  -9.436  1.00 25.91  ? 368 SER   A O   1 
ATOM   1412 C  CB  . SER   A 1 189 ? 22.693 -5.138  -7.455  1.00 25.13  ? 368 SER   A CB  1 
ATOM   1413 O  OG  . SER   A 1 189 ? 22.323 -4.912  -6.104  1.00 25.87  ? 368 SER   A OG  1 
ATOM   1414 N  N   . ASP   A 1 190 ? 24.911 -4.382  -9.889  1.00 26.06  ? 369 ASP   A N   1 
ATOM   1415 C  CA  . ASP   A 1 190 ? 25.112 -4.604  -11.315 1.00 26.83  ? 369 ASP   A CA  1 
ATOM   1416 C  C   . ASP   A 1 190 ? 26.527 -5.122  -11.581 1.00 27.40  ? 369 ASP   A C   1 
ATOM   1417 O  O   . ASP   A 1 190 ? 27.221 -5.551  -10.659 1.00 26.25  ? 369 ASP   A O   1 
ATOM   1418 C  CB  . ASP   A 1 190 ? 24.709 -3.385  -12.154 1.00 26.53  ? 369 ASP   A CB  1 
ATOM   1419 C  CG  . ASP   A 1 190 ? 25.628 -2.180  -12.015 1.00 27.10  ? 369 ASP   A CG  1 
ATOM   1420 O  OD1 . ASP   A 1 190 ? 26.641 -2.277  -11.291 1.00 26.43  ? 369 ASP   A OD1 1 
ATOM   1421 O  OD2 . ASP   A 1 190 ? 25.320 -1.148  -12.632 1.00 26.48  ? 369 ASP   A OD2 1 
ATOM   1422 N  N   . ARG   A 1 191 ? 26.943 -5.058  -12.854 1.00 27.40  ? 370 ARG   A N   1 
ATOM   1423 C  CA  . ARG   A 1 191 ? 28.156 -5.699  -13.339 1.00 27.92  ? 370 ARG   A CA  1 
ATOM   1424 C  C   . ARG   A 1 191 ? 29.407 -5.034  -12.765 1.00 26.77  ? 370 ARG   A C   1 
ATOM   1425 O  O   . ARG   A 1 191 ? 30.510 -5.547  -12.937 1.00 27.34  ? 370 ARG   A O   1 
ATOM   1426 C  CB  . ARG   A 1 191 ? 28.212 -5.689  -14.870 1.00 30.02  ? 370 ARG   A CB  1 
ATOM   1427 C  CG  . ARG   A 1 191 ? 28.236 -4.297  -15.488 1.00 33.01  ? 370 ARG   A CG  1 
ATOM   1428 C  CD  . ARG   A 1 191 ? 29.194 -4.214  -16.664 1.00 38.31  ? 370 ARG   A CD  1 
ATOM   1429 N  NE  . ARG   A 1 191 ? 29.021 -5.237  -17.684 1.00 41.43  ? 370 ARG   A NE  1 
ATOM   1430 C  CZ  . ARG   A 1 191 ? 29.908 -5.519  -18.634 1.00 43.48  ? 370 ARG   A CZ  1 
ATOM   1431 N  NH1 . ARG   A 1 191 ? 31.079 -4.908  -18.658 1.00 45.06  ? 370 ARG   A NH1 1 
ATOM   1432 N  NH2 . ARG   A 1 191 ? 29.624 -6.429  -19.549 1.00 45.10  ? 370 ARG   A NH2 1 
ATOM   1433 N  N   . ARG   A 1 192 ? 29.230 -3.893  -12.092 1.00 25.52  ? 371 ARG   A N   1 
ATOM   1434 C  CA  . ARG   A 1 192 ? 30.333 -3.205  -11.439 1.00 25.94  ? 371 ARG   A CA  1 
ATOM   1435 C  C   . ARG   A 1 192 ? 30.955 -4.075  -10.347 1.00 25.11  ? 371 ARG   A C   1 
ATOM   1436 O  O   . ARG   A 1 192 ? 32.120 -3.885  -10.010 1.00 25.36  ? 371 ARG   A O   1 
ATOM   1437 C  CB  . ARG   A 1 192 ? 29.882 -1.852  -10.879 1.00 26.90  ? 371 ARG   A CB  1 
ATOM   1438 C  CG  . ARG   A 1 192 ? 29.698 -0.779  -11.943 1.00 28.67  ? 371 ARG   A CG  1 
ATOM   1439 C  CD  . ARG   A 1 192 ? 29.118 0.513   -11.403 1.00 29.34  ? 371 ARG   A CD  1 
ATOM   1440 N  NE  . ARG   A 1 192 ? 27.717 0.382   -11.027 1.00 30.68  ? 371 ARG   A NE  1 
ATOM   1441 C  CZ  . ARG   A 1 192 ? 26.964 1.373   -10.560 1.00 30.38  ? 371 ARG   A CZ  1 
ATOM   1442 N  NH1 . ARG   A 1 192 ? 27.476 2.581   -10.398 1.00 31.13  ? 371 ARG   A NH1 1 
ATOM   1443 N  NH2 . ARG   A 1 192 ? 25.699 1.151   -10.255 1.00 30.86  ? 371 ARG   A NH2 1 
ATOM   1444 N  N   . ASN   A 1 193 ? 30.186 -5.026  -9.798  1.00 24.21  ? 372 ASN   A N   1 
ATOM   1445 C  CA  . ASN   A 1 193 ? 30.674 -5.800  -8.666  1.00 24.55  ? 372 ASN   A CA  1 
ATOM   1446 C  C   . ASN   A 1 193 ? 30.467 -7.302  -8.868  1.00 24.77  ? 372 ASN   A C   1 
ATOM   1447 O  O   . ASN   A 1 193 ? 29.626 -7.902  -8.197  1.00 25.07  ? 372 ASN   A O   1 
ATOM   1448 C  CB  . ASN   A 1 193 ? 30.058 -5.334  -7.342  1.00 24.42  ? 372 ASN   A CB  1 
ATOM   1449 C  CG  . ASN   A 1 193 ? 30.608 -4.011  -6.855  1.00 24.77  ? 372 ASN   A CG  1 
ATOM   1450 O  OD1 . ASN   A 1 193 ? 31.818 -3.856  -6.698  1.00 24.74  ? 372 ASN   A OD1 1 
ATOM   1451 N  ND2 . ASN   A 1 193 ? 29.726 -3.056  -6.605  1.00 23.89  ? 372 ASN   A ND2 1 
ATOM   1452 N  N   . PRO   A 1 194 ? 31.260 -7.974  -9.738  1.00 25.04  ? 373 PRO   A N   1 
ATOM   1453 C  CA  . PRO   A 1 194 ? 31.327 -9.435  -9.729  1.00 24.95  ? 373 PRO   A CA  1 
ATOM   1454 C  C   . PRO   A 1 194 ? 31.928 -9.860  -8.392  1.00 25.22  ? 373 PRO   A C   1 
ATOM   1455 O  O   . PRO   A 1 194 ? 32.807 -9.178  -7.867  1.00 25.53  ? 373 PRO   A O   1 
ATOM   1456 C  CB  . PRO   A 1 194 ? 32.294 -9.784  -10.872 1.00 25.27  ? 373 PRO   A CB  1 
ATOM   1457 C  CG  . PRO   A 1 194 ? 32.351 -8.533  -11.723 1.00 25.46  ? 373 PRO   A CG  1 
ATOM   1458 C  CD  . PRO   A 1 194 ? 32.134 -7.381  -10.762 1.00 25.00  ? 373 PRO   A CD  1 
ATOM   1459 N  N   . HIS   A 1 195 ? 31.436 -10.979 -7.846  1.00 25.44  ? 374 HIS   A N   1 
ATOM   1460 C  CA  . HIS   A 1 195 ? 31.840 -11.423 -6.522  1.00 26.31  ? 374 HIS   A CA  1 
ATOM   1461 C  C   . HIS   A 1 195 ? 31.648 -12.929 -6.373  1.00 27.26  ? 374 HIS   A C   1 
ATOM   1462 O  O   . HIS   A 1 195 ? 30.837 -13.538 -7.071  1.00 27.26  ? 374 HIS   A O   1 
ATOM   1463 C  CB  . HIS   A 1 195 ? 31.097 -10.648 -5.424  1.00 25.89  ? 374 HIS   A CB  1 
ATOM   1464 C  CG  . HIS   A 1 195 ? 29.606 -10.701 -5.526  1.00 25.56  ? 374 HIS   A CG  1 
ATOM   1465 N  ND1 . HIS   A 1 195 ? 28.885 -9.931  -6.413  1.00 25.22  ? 374 HIS   A ND1 1 
ATOM   1466 C  CD2 . HIS   A 1 195 ? 28.703 -11.407 -4.830  1.00 25.28  ? 374 HIS   A CD2 1 
ATOM   1467 C  CE1 . HIS   A 1 195 ? 27.591 -10.185 -6.264  1.00 24.94  ? 374 HIS   A CE1 1 
ATOM   1468 N  NE2 . HIS   A 1 195 ? 27.457 -11.075 -5.303  1.00 24.75  ? 374 HIS   A NE2 1 
ATOM   1469 N  N   . GLU   A 1 196 ? 32.395 -13.504 -5.423  1.00 27.91  ? 375 GLU   A N   1 
ATOM   1470 C  CA  . GLU   A 1 196 ? 32.377 -14.932 -5.157  1.00 28.76  ? 375 GLU   A CA  1 
ATOM   1471 C  C   . GLU   A 1 196 ? 32.464 -15.161 -3.650  1.00 28.36  ? 375 GLU   A C   1 
ATOM   1472 O  O   . GLU   A 1 196 ? 33.070 -14.370 -2.930  1.00 29.18  ? 375 GLU   A O   1 
ATOM   1473 C  CB  . GLU   A 1 196 ? 33.538 -15.619 -5.886  1.00 29.65  ? 375 GLU   A CB  1 
ATOM   1474 C  CG  . GLU   A 1 196 ? 34.908 -15.292 -5.306  1.00 32.61  ? 375 GLU   A CG  1 
ATOM   1475 C  CD  . GLU   A 1 196 ? 36.123 -15.725 -6.112  1.00 34.60  ? 375 GLU   A CD  1 
ATOM   1476 O  OE1 . GLU   A 1 196 ? 37.240 -15.678 -5.561  1.00 36.44  ? 375 GLU   A OE1 1 
ATOM   1477 O  OE2 . GLU   A 1 196 ? 35.959 -16.078 -7.293  1.00 36.21  ? 375 GLU   A OE2 1 
ATOM   1478 N  N   . VAL   A 1 197 ? 31.842 -16.248 -3.184  1.00 29.31  ? 376 VAL   A N   1 
ATOM   1479 C  CA  . VAL   A 1 197 ? 32.026 -16.704 -1.817  1.00 29.19  ? 376 VAL   A CA  1 
ATOM   1480 C  C   . VAL   A 1 197 ? 33.046 -17.839 -1.841  1.00 30.47  ? 376 VAL   A C   1 
ATOM   1481 O  O   . VAL   A 1 197 ? 32.819 -18.864 -2.482  1.00 30.03  ? 376 VAL   A O   1 
ATOM   1482 C  CB  . VAL   A 1 197 ? 30.694 -17.127 -1.161  1.00 30.13  ? 376 VAL   A CB  1 
ATOM   1483 C  CG1 . VAL   A 1 197 ? 30.893 -17.643 0.258   1.00 29.87  ? 376 VAL   A CG1 1 
ATOM   1484 C  CG2 . VAL   A 1 197 ? 29.676 -15.995 -1.167  1.00 29.48  ? 376 VAL   A CG2 1 
ATOM   1485 N  N   . GLN   A 1 198 ? 34.178 -17.620 -1.158  1.00 30.94  ? 377 GLN   A N   1 
ATOM   1486 C  CA  . GLN   A 1 198 ? 35.235 -18.611 -1.008  1.00 32.60  ? 377 GLN   A CA  1 
ATOM   1487 C  C   . GLN   A 1 198 ? 34.689 -19.807 -0.228  1.00 30.88  ? 377 GLN   A C   1 
ATOM   1488 O  O   . GLN   A 1 198 ? 33.755 -19.654 0.557   1.00 29.80  ? 377 GLN   A O   1 
ATOM   1489 C  CB  . GLN   A 1 198 ? 36.421 -18.011 -0.248  1.00 35.78  ? 377 GLN   A CB  1 
ATOM   1490 C  CG  . GLN   A 1 198 ? 37.155 -16.887 -0.971  1.00 40.26  ? 377 GLN   A CG  1 
ATOM   1491 C  CD  . GLN   A 1 198 ? 38.138 -17.367 -2.011  1.00 43.63  ? 377 GLN   A CD  1 
ATOM   1492 O  OE1 . GLN   A 1 198 ? 38.983 -18.223 -1.753  1.00 46.65  ? 377 GLN   A OE1 1 
ATOM   1493 N  NE2 . GLN   A 1 198 ? 38.035 -16.813 -3.208  1.00 45.13  ? 377 GLN   A NE2 1 
ATOM   1494 N  N   . PRO   A 1 199 ? 35.249 -21.029 -0.407  1.00 30.35  ? 378 PRO   A N   1 
ATOM   1495 C  CA  . PRO   A 1 199 ? 34.766 -22.214 0.307   1.00 29.96  ? 378 PRO   A CA  1 
ATOM   1496 C  C   . PRO   A 1 199 ? 34.673 -21.989 1.816   1.00 28.78  ? 378 PRO   A C   1 
ATOM   1497 O  O   . PRO   A 1 199 ? 35.581 -21.421 2.420   1.00 29.10  ? 378 PRO   A O   1 
ATOM   1498 C  CB  . PRO   A 1 199 ? 35.838 -23.274 0.003   1.00 30.46  ? 378 PRO   A CB  1 
ATOM   1499 C  CG  . PRO   A 1 199 ? 36.412 -22.853 -1.332  1.00 30.90  ? 378 PRO   A CG  1 
ATOM   1500 C  CD  . PRO   A 1 199 ? 36.371 -21.337 -1.310  1.00 31.15  ? 378 PRO   A CD  1 
ATOM   1501 N  N   . ALA   A 1 200 ? 33.557 -22.431 2.404   1.00 28.28  ? 379 ALA   A N   1 
ATOM   1502 C  CA  . ALA   A 1 200 ? 33.319 -22.306 3.832   1.00 28.85  ? 379 ALA   A CA  1 
ATOM   1503 C  C   . ALA   A 1 200 ? 33.502 -23.669 4.494   1.00 29.42  ? 379 ALA   A C   1 
ATOM   1504 O  O   . ALA   A 1 200 ? 33.058 -24.681 3.958   1.00 29.57  ? 379 ALA   A O   1 
ATOM   1505 C  CB  . ALA   A 1 200 ? 31.934 -21.756 4.072   1.00 29.03  ? 379 ALA   A CB  1 
ATOM   1506 N  N   . TYR   A 1 201 ? 34.155 -23.676 5.661   1.00 30.58  ? 380 TYR   A N   1 
ATOM   1507 C  CA  . TYR   A 1 201 ? 34.471 -24.903 6.377   1.00 31.99  ? 380 TYR   A CA  1 
ATOM   1508 C  C   . TYR   A 1 201 ? 33.815 -24.882 7.756   1.00 31.82  ? 380 TYR   A C   1 
ATOM   1509 O  O   . TYR   A 1 201 ? 34.171 -25.664 8.637   1.00 31.89  ? 380 TYR   A O   1 
ATOM   1510 C  CB  . TYR   A 1 201 ? 35.984 -25.141 6.382   1.00 32.74  ? 380 TYR   A CB  1 
ATOM   1511 C  CG  . TYR   A 1 201 ? 36.548 -25.360 5.002   1.00 34.10  ? 380 TYR   A CG  1 
ATOM   1512 C  CD1 . TYR   A 1 201 ? 36.363 -26.563 4.336   1.00 35.02  ? 380 TYR   A CD1 1 
ATOM   1513 C  CD2 . TYR   A 1 201 ? 37.217 -24.345 4.335   1.00 34.95  ? 380 TYR   A CD2 1 
ATOM   1514 C  CE1 . TYR   A 1 201 ? 36.862 -26.764 3.058   1.00 36.26  ? 380 TYR   A CE1 1 
ATOM   1515 C  CE2 . TYR   A 1 201 ? 37.715 -24.527 3.055   1.00 35.90  ? 380 TYR   A CE2 1 
ATOM   1516 C  CZ  . TYR   A 1 201 ? 37.535 -25.740 2.414   1.00 37.00  ? 380 TYR   A CZ  1 
ATOM   1517 O  OH  . TYR   A 1 201 ? 38.028 -25.924 1.145   1.00 38.70  ? 380 TYR   A OH  1 
ATOM   1518 N  N   . ALA   A 1 202 ? 32.846 -23.975 7.908   1.00 31.12  ? 381 ALA   A N   1 
ATOM   1519 C  CA  . ALA   A 1 202 ? 31.935 -23.927 9.038   1.00 30.70  ? 381 ALA   A CA  1 
ATOM   1520 C  C   . ALA   A 1 202 ? 30.598 -23.389 8.539   1.00 30.19  ? 381 ALA   A C   1 
ATOM   1521 O  O   . ALA   A 1 202 ? 30.538 -22.791 7.466   1.00 29.41  ? 381 ALA   A O   1 
ATOM   1522 C  CB  . ALA   A 1 202 ? 32.509 -23.050 10.126  1.00 31.34  ? 381 ALA   A CB  1 
ATOM   1523 N  N   . THR   A 1 203 ? 29.531 -23.617 9.314   1.00 29.31  ? 382 THR   A N   1 
ATOM   1524 C  CA  . THR   A 1 203 ? 28.213 -23.122 8.951   1.00 29.06  ? 382 THR   A CA  1 
ATOM   1525 C  C   . THR   A 1 203 ? 28.266 -21.600 8.842   1.00 27.23  ? 382 THR   A C   1 
ATOM   1526 O  O   . THR   A 1 203 ? 28.659 -20.921 9.789   1.00 27.26  ? 382 THR   A O   1 
ATOM   1527 C  CB  . THR   A 1 203 ? 27.141 -23.605 9.937   1.00 30.23  ? 382 THR   A CB  1 
ATOM   1528 O  OG1 . THR   A 1 203 ? 27.228 -25.027 10.039  1.00 30.02  ? 382 THR   A OG1 1 
ATOM   1529 C  CG2 . THR   A 1 203 ? 25.742 -23.200 9.523   1.00 30.21  ? 382 THR   A CG2 1 
ATOM   1530 N  N   . ARG   A 1 204 ? 27.861 -21.085 7.674   1.00 26.07  ? 383 ARG   A N   1 
ATOM   1531 C  CA  . ARG   A 1 204 ? 27.977 -19.675 7.336   1.00 25.78  ? 383 ARG   A CA  1 
ATOM   1532 C  C   . ARG   A 1 204 ? 26.596 -19.125 6.989   1.00 25.27  ? 383 ARG   A C   1 
ATOM   1533 O  O   . ARG   A 1 204 ? 25.958 -19.596 6.050   1.00 24.69  ? 383 ARG   A O   1 
ATOM   1534 C  CB  . ARG   A 1 204 ? 28.937 -19.522 6.150   1.00 25.47  ? 383 ARG   A CB  1 
ATOM   1535 C  CG  . ARG   A 1 204 ? 29.224 -18.089 5.721   1.00 25.51  ? 383 ARG   A CG  1 
ATOM   1536 C  CD  . ARG   A 1 204 ? 29.979 -18.112 4.401   1.00 25.11  ? 383 ARG   A CD  1 
ATOM   1537 N  NE  . ARG   A 1 204 ? 30.458 -16.833 3.885   1.00 23.76  ? 383 ARG   A NE  1 
ATOM   1538 C  CZ  . ARG   A 1 204 ? 29.718 -15.915 3.268   1.00 23.69  ? 383 ARG   A CZ  1 
ATOM   1539 N  NH1 . ARG   A 1 204 ? 28.410 -16.073 3.141   1.00 23.40  ? 383 ARG   A NH1 1 
ATOM   1540 N  NH2 . ARG   A 1 204 ? 30.296 -14.831 2.778   1.00 23.05  ? 383 ARG   A NH2 1 
ATOM   1541 N  N   . TYR   A 1 205 ? 26.147 -18.123 7.755   1.00 25.22  ? 384 TYR   A N   1 
ATOM   1542 C  CA  . TYR   A 1 205 ? 24.855 -17.496 7.527   1.00 26.10  ? 384 TYR   A CA  1 
ATOM   1543 C  C   . TYR   A 1 205 ? 25.032 -16.054 7.065   1.00 26.00  ? 384 TYR   A C   1 
ATOM   1544 O  O   . TYR   A 1 205 ? 25.954 -15.363 7.496   1.00 26.38  ? 384 TYR   A O   1 
ATOM   1545 C  CB  . TYR   A 1 205 ? 24.016 -17.486 8.806   1.00 27.06  ? 384 TYR   A CB  1 
ATOM   1546 C  CG  . TYR   A 1 205 ? 23.590 -18.835 9.327   1.00 28.62  ? 384 TYR   A CG  1 
ATOM   1547 C  CD1 . TYR   A 1 205 ? 22.784 -19.675 8.574   1.00 30.06  ? 384 TYR   A CD1 1 
ATOM   1548 C  CD2 . TYR   A 1 205 ? 23.971 -19.259 10.590  1.00 28.81  ? 384 TYR   A CD2 1 
ATOM   1549 C  CE1 . TYR   A 1 205 ? 22.375 -20.907 9.057   1.00 30.16  ? 384 TYR   A CE1 1 
ATOM   1550 C  CE2 . TYR   A 1 205 ? 23.575 -20.490 11.088  1.00 30.41  ? 384 TYR   A CE2 1 
ATOM   1551 C  CZ  . TYR   A 1 205 ? 22.774 -21.315 10.318  1.00 30.97  ? 384 TYR   A CZ  1 
ATOM   1552 O  OH  . TYR   A 1 205 ? 22.377 -22.534 10.805  1.00 34.25  ? 384 TYR   A OH  1 
ATOM   1553 N  N   . ALA   A 1 206 ? 24.109 -15.616 6.202   1.00 26.05  ? 385 ALA   A N   1 
ATOM   1554 C  CA  . ALA   A 1 206 ? 24.013 -14.240 5.745   1.00 26.04  ? 385 ALA   A CA  1 
ATOM   1555 C  C   . ALA   A 1 206 ? 22.551 -13.925 5.437   1.00 25.25  ? 385 ALA   A C   1 
ATOM   1556 O  O   . ALA   A 1 206 ? 21.771 -14.826 5.132   1.00 25.35  ? 385 ALA   A O   1 
ATOM   1557 C  CB  . ALA   A 1 206 ? 24.884 -14.038 4.528   1.00 26.18  ? 385 ALA   A CB  1 
ATOM   1558 N  N   . ILE   A 1 207 ? 22.198 -12.639 5.523   1.00 24.61  ? 386 ILE   A N   1 
ATOM   1559 C  CA  . ILE   A 1 207 ? 20.863 -12.167 5.184   1.00 24.26  ? 386 ILE   A CA  1 
ATOM   1560 C  C   . ILE   A 1 207 ? 21.010 -11.011 4.198   1.00 24.04  ? 386 ILE   A C   1 
ATOM   1561 O  O   . ILE   A 1 207 ? 21.669 -10.022 4.511   1.00 23.78  ? 386 ILE   A O   1 
ATOM   1562 C  CB  . ILE   A 1 207 ? 20.087 -11.747 6.450   1.00 24.14  ? 386 ILE   A CB  1 
ATOM   1563 C  CG1 . ILE   A 1 207 ? 19.976 -12.896 7.458   1.00 24.38  ? 386 ILE   A CG1 1 
ATOM   1564 C  CG2 . ILE   A 1 207 ? 18.721 -11.177 6.086   1.00 23.48  ? 386 ILE   A CG2 1 
ATOM   1565 C  CD1 . ILE   A 1 207 ? 19.368 -12.502 8.791   1.00 24.81  ? 386 ILE   A CD1 1 
ATOM   1566 N  N   . THR   A 1 208 ? 20.381 -11.147 3.021   1.00 23.49  ? 387 THR   A N   1 
ATOM   1567 C  CA  . THR   A 1 208 ? 20.529 -10.183 1.941   1.00 23.92  ? 387 THR   A CA  1 
ATOM   1568 C  C   . THR   A 1 208 ? 19.171 -9.624  1.519   1.00 24.00  ? 387 THR   A C   1 
ATOM   1569 O  O   . THR   A 1 208 ? 18.205 -10.373 1.372   1.00 23.54  ? 387 THR   A O   1 
ATOM   1570 C  CB  . THR   A 1 208 ? 21.196 -10.818 0.714   1.00 24.23  ? 387 THR   A CB  1 
ATOM   1571 O  OG1 . THR   A 1 208 ? 22.437 -11.408 1.097   1.00 25.04  ? 387 THR   A OG1 1 
ATOM   1572 C  CG2 . THR   A 1 208 ? 21.441 -9.827  -0.404  1.00 24.78  ? 387 THR   A CG2 1 
ATOM   1573 N  N   . VAL   A 1 209 ? 19.125 -8.302  1.309   1.00 23.37  ? 388 VAL   A N   1 
ATOM   1574 C  CA  . VAL   A 1 209 ? 18.035 -7.664  0.584   1.00 24.59  ? 388 VAL   A CA  1 
ATOM   1575 C  C   . VAL   A 1 209 ? 18.626 -6.888  -0.590  1.00 25.05  ? 388 VAL   A C   1 
ATOM   1576 O  O   . VAL   A 1 209 ? 19.776 -6.448  -0.541  1.00 24.45  ? 388 VAL   A O   1 
ATOM   1577 C  CB  . VAL   A 1 209 ? 17.163 -6.750  1.471   1.00 25.62  ? 388 VAL   A CB  1 
ATOM   1578 C  CG1 . VAL   A 1 209 ? 16.528 -7.498  2.634   1.00 26.92  ? 388 VAL   A CG1 1 
ATOM   1579 C  CG2 . VAL   A 1 209 ? 17.925 -5.532  1.970   1.00 26.50  ? 388 VAL   A CG2 1 
ATOM   1580 N  N   . TRP   A 1 210 ? 17.820 -6.731  -1.644  1.00 24.46  ? 389 TRP   A N   1 
ATOM   1581 C  CA  . TRP   A 1 210 ? 18.195 -5.899  -2.774  1.00 24.79  ? 389 TRP   A CA  1 
ATOM   1582 C  C   . TRP   A 1 210 ? 17.213 -4.740  -2.888  1.00 25.69  ? 389 TRP   A C   1 
ATOM   1583 O  O   . TRP   A 1 210 ? 16.002 -4.949  -2.844  1.00 24.64  ? 389 TRP   A O   1 
ATOM   1584 C  CB  . TRP   A 1 210 ? 18.229 -6.714  -4.072  1.00 24.63  ? 389 TRP   A CB  1 
ATOM   1585 C  CG  . TRP   A 1 210 ? 19.309 -7.748  -4.144  1.00 24.60  ? 389 TRP   A CG  1 
ATOM   1586 C  CD1 . TRP   A 1 210 ? 20.518 -7.623  -4.761  1.00 24.70  ? 389 TRP   A CD1 1 
ATOM   1587 C  CD2 . TRP   A 1 210 ? 19.261 -9.089  -3.623  1.00 24.73  ? 389 TRP   A CD2 1 
ATOM   1588 N  NE1 . TRP   A 1 210 ? 21.236 -8.783  -4.643  1.00 25.43  ? 389 TRP   A NE1 1 
ATOM   1589 C  CE2 . TRP   A 1 210 ? 20.492 -9.701  -3.950  1.00 24.75  ? 389 TRP   A CE2 1 
ATOM   1590 C  CE3 . TRP   A 1 210 ? 18.310 -9.827  -2.908  1.00 25.70  ? 389 TRP   A CE3 1 
ATOM   1591 C  CZ2 . TRP   A 1 210 ? 20.792 -11.014 -3.586  1.00 25.84  ? 389 TRP   A CZ2 1 
ATOM   1592 C  CZ3 . TRP   A 1 210 ? 18.608 -11.124 -2.544  1.00 26.54  ? 389 TRP   A CZ3 1 
ATOM   1593 C  CH2 . TRP   A 1 210 ? 19.831 -11.708 -2.883  1.00 26.46  ? 389 TRP   A CH2 1 
ATOM   1594 N  N   . TYR   A 1 211 ? 17.757 -3.529  -3.045  1.00 25.77  ? 390 TYR   A N   1 
ATOM   1595 C  CA  . TYR   A 1 211 ? 16.952 -2.331  -3.220  1.00 26.20  ? 390 TYR   A CA  1 
ATOM   1596 C  C   . TYR   A 1 211 ? 16.775 -2.048  -4.708  1.00 27.40  ? 390 TYR   A C   1 
ATOM   1597 O  O   . TYR   A 1 211 ? 17.705 -2.235  -5.490  1.00 26.96  ? 390 TYR   A O   1 
ATOM   1598 C  CB  . TYR   A 1 211 ? 17.544 -1.154  -2.439  1.00 25.89  ? 390 TYR   A CB  1 
ATOM   1599 C  CG  . TYR   A 1 211 ? 17.418 -1.321  -0.947  1.00 25.53  ? 390 TYR   A CG  1 
ATOM   1600 C  CD1 . TYR   A 1 211 ? 18.403 -1.964  -0.208  1.00 25.15  ? 390 TYR   A CD1 1 
ATOM   1601 C  CD2 . TYR   A 1 211 ? 16.267 -0.919  -0.288  1.00 25.60  ? 390 TYR   A CD2 1 
ATOM   1602 C  CE1 . TYR   A 1 211 ? 18.266 -2.153  1.159   1.00 25.18  ? 390 TYR   A CE1 1 
ATOM   1603 C  CE2 . TYR   A 1 211 ? 16.113 -1.103  1.076   1.00 25.50  ? 390 TYR   A CE2 1 
ATOM   1604 C  CZ  . TYR   A 1 211 ? 17.114 -1.726  1.800   1.00 24.91  ? 390 TYR   A CZ  1 
ATOM   1605 O  OH  . TYR   A 1 211 ? 16.952 -1.900  3.152   1.00 25.87  ? 390 TYR   A OH  1 
ATOM   1606 N  N   . PHE   A 1 212 ? 15.565 -1.598  -5.067  1.00 28.12  ? 391 PHE   A N   1 
ATOM   1607 C  CA  . PHE   A 1 212 ? 15.188 -1.342  -6.447  1.00 29.89  ? 391 PHE   A CA  1 
ATOM   1608 C  C   . PHE   A 1 212 ? 15.387 0.130   -6.784  1.00 30.16  ? 391 PHE   A C   1 
ATOM   1609 O  O   . PHE   A 1 212 ? 15.126 1.004   -5.959  1.00 30.00  ? 391 PHE   A O   1 
ATOM   1610 C  CB  . PHE   A 1 212 ? 13.715 -1.688  -6.686  1.00 30.48  ? 391 PHE   A CB  1 
ATOM   1611 C  CG  . PHE   A 1 212 ? 13.353 -3.143  -6.526  1.00 32.13  ? 391 PHE   A CG  1 
ATOM   1612 C  CD1 . PHE   A 1 212 ? 13.960 -4.119  -7.302  1.00 32.89  ? 391 PHE   A CD1 1 
ATOM   1613 C  CD2 . PHE   A 1 212 ? 12.381 -3.532  -5.615  1.00 33.16  ? 391 PHE   A CD2 1 
ATOM   1614 C  CE1 . PHE   A 1 212 ? 13.620 -5.456  -7.153  1.00 33.93  ? 391 PHE   A CE1 1 
ATOM   1615 C  CE2 . PHE   A 1 212 ? 12.041 -4.869  -5.469  1.00 33.71  ? 391 PHE   A CE2 1 
ATOM   1616 C  CZ  . PHE   A 1 212 ? 12.665 -5.829  -6.234  1.00 33.53  ? 391 PHE   A CZ  1 
ATOM   1617 N  N   . ASP   A 1 213 ? 15.852 0.380   -8.012  1.00 30.57  ? 392 ASP   A N   1 
ATOM   1618 C  CA  . ASP   A 1 213 ? 15.740 1.694   -8.620  1.00 30.94  ? 392 ASP   A CA  1 
ATOM   1619 C  C   . ASP   A 1 213 ? 14.392 1.761   -9.330  1.00 31.67  ? 392 ASP   A C   1 
ATOM   1620 O  O   . ASP   A 1 213 ? 14.096 0.909   -10.165 1.00 30.59  ? 392 ASP   A O   1 
ATOM   1621 C  CB  . ASP   A 1 213 ? 16.890 1.970   -9.590  1.00 31.43  ? 392 ASP   A CB  1 
ATOM   1622 C  CG  . ASP   A 1 213 ? 16.666 3.216   -10.430 1.00 31.60  ? 392 ASP   A CG  1 
ATOM   1623 O  OD1 . ASP   A 1 213 ? 16.738 4.328   -9.864  1.00 31.37  ? 392 ASP   A OD1 1 
ATOM   1624 O  OD2 . ASP   A 1 213 ? 16.391 3.063   -11.637 1.00 30.75  ? 392 ASP   A OD2 1 
ATOM   1625 N  N   . ALA   A 1 214 ? 13.598 2.782   -8.985  1.00 32.76  ? 393 ALA   A N   1 
ATOM   1626 C  CA  . ALA   A 1 214 ? 12.241 2.950   -9.483  1.00 33.90  ? 393 ALA   A CA  1 
ATOM   1627 C  C   . ALA   A 1 214 ? 12.216 2.871   -11.008 1.00 34.59  ? 393 ALA   A C   1 
ATOM   1628 O  O   . ALA   A 1 214 ? 11.389 2.160   -11.576 1.00 34.68  ? 393 ALA   A O   1 
ATOM   1629 C  CB  . ALA   A 1 214 ? 11.669 4.258   -8.991  1.00 33.53  ? 393 ALA   A CB  1 
ATOM   1630 N  N   . ASP   A 1 215 ? 13.144 3.596   -11.646 1.00 35.25  ? 394 ASP   A N   1 
ATOM   1631 C  CA  . ASP   A 1 215 ? 13.193 3.750   -13.092 1.00 36.87  ? 394 ASP   A CA  1 
ATOM   1632 C  C   . ASP   A 1 215 ? 13.468 2.401   -13.757 1.00 36.05  ? 394 ASP   A C   1 
ATOM   1633 O  O   . ASP   A 1 215 ? 12.714 1.976   -14.630 1.00 34.72  ? 394 ASP   A O   1 
ATOM   1634 C  CB  . ASP   A 1 215 ? 14.213 4.819   -13.500 1.00 39.10  ? 394 ASP   A CB  1 
ATOM   1635 C  CG  . ASP   A 1 215 ? 14.019 6.152   -12.794 1.00 41.17  ? 394 ASP   A CG  1 
ATOM   1636 O  OD1 . ASP   A 1 215 ? 13.034 6.850   -13.114 1.00 39.86  ? 394 ASP   A OD1 1 
ATOM   1637 O  OD2 . ASP   A 1 215 ? 14.848 6.474   -11.913 1.00 43.54  ? 394 ASP   A OD2 1 
ATOM   1638 N  N   . GLU   A 1 216 ? 14.544 1.733   -13.321 1.00 35.61  ? 395 GLU   A N   1 
ATOM   1639 C  CA  . GLU   A 1 216 ? 15.000 0.484   -13.912 1.00 36.29  ? 395 GLU   A CA  1 
ATOM   1640 C  C   . GLU   A 1 216 ? 13.971 -0.617  -13.656 1.00 36.81  ? 395 GLU   A C   1 
ATOM   1641 O  O   . GLU   A 1 216 ? 13.694 -1.422  -14.544 1.00 36.68  ? 395 GLU   A O   1 
ATOM   1642 C  CB  . GLU   A 1 216 ? 16.383 0.119   -13.366 1.00 36.71  ? 395 GLU   A CB  1 
ATOM   1643 C  CG  . GLU   A 1 216 ? 17.051 -1.044  -14.083 1.00 37.90  ? 395 GLU   A CG  1 
ATOM   1644 C  CD  . GLU   A 1 216 ? 18.346 -1.521  -13.443 1.00 39.90  ? 395 GLU   A CD  1 
ATOM   1645 O  OE1 . GLU   A 1 216 ? 19.278 -0.703  -13.317 1.00 42.66  ? 395 GLU   A OE1 1 
ATOM   1646 O  OE2 . GLU   A 1 216 ? 18.421 -2.709  -13.066 1.00 38.38  ? 395 GLU   A OE2 1 
ATOM   1647 N  N   . ARG   A 1 217 ? 13.417 -0.635  -12.436 1.00 37.29  ? 396 ARG   A N   1 
ATOM   1648 C  CA  . ARG   A 1 217 ? 12.392 -1.584  -12.024 1.00 38.84  ? 396 ARG   A CA  1 
ATOM   1649 C  C   . ARG   A 1 217 ? 11.183 -1.475  -12.954 1.00 39.01  ? 396 ARG   A C   1 
ATOM   1650 O  O   . ARG   A 1 217 ? 10.656 -2.491  -13.404 1.00 39.27  ? 396 ARG   A O   1 
ATOM   1651 C  CB  . ARG   A 1 217 ? 12.009 -1.327  -10.561 1.00 41.35  ? 396 ARG   A CB  1 
ATOM   1652 C  CG  . ARG   A 1 217 ? 10.793 -2.090  -10.051 1.00 44.92  ? 396 ARG   A CG  1 
ATOM   1653 C  CD  . ARG   A 1 217 ? 11.005 -3.561  -9.742  1.00 48.53  ? 396 ARG   A CD  1 
ATOM   1654 N  NE  . ARG   A 1 217 ? 9.879  -4.089  -8.978  1.00 52.05  ? 396 ARG   A NE  1 
ATOM   1655 C  CZ  . ARG   A 1 217 ? 9.753  -5.346  -8.560  1.00 52.79  ? 396 ARG   A CZ  1 
ATOM   1656 N  NH1 . ARG   A 1 217 ? 10.670 -6.248  -8.867  1.00 52.01  ? 396 ARG   A NH1 1 
ATOM   1657 N  NH2 . ARG   A 1 217 ? 8.703  -5.697  -7.837  1.00 51.12  ? 396 ARG   A NH2 1 
ATOM   1658 N  N   . ALA   A 1 218 ? 10.767 -0.235  -13.242 1.00 38.64  ? 397 ALA   A N   1 
ATOM   1659 C  CA  . ALA   A 1 218 ? 9.604  0.033   -14.075 1.00 41.06  ? 397 ALA   A CA  1 
ATOM   1660 C  C   . ALA   A 1 218 ? 9.849  -0.444  -15.505 1.00 42.44  ? 397 ALA   A C   1 
ATOM   1661 O  O   . ALA   A 1 218 ? 8.942  -0.978  -16.143 1.00 42.17  ? 397 ALA   A O   1 
ATOM   1662 C  CB  . ALA   A 1 218 ? 9.258  1.503   -14.029 1.00 39.93  ? 397 ALA   A CB  1 
ATOM   1663 N  N   . ARG   A 1 219 ? 11.083 -0.255  -15.990 1.00 43.20  ? 398 ARG   A N   1 
ATOM   1664 C  CA  . ARG   A 1 219 ? 11.451 -0.609  -17.352 1.00 45.05  ? 398 ARG   A CA  1 
ATOM   1665 C  C   . ARG   A 1 219 ? 11.672 -2.115  -17.466 1.00 46.51  ? 398 ARG   A C   1 
ATOM   1666 O  O   . ARG   A 1 219 ? 11.597 -2.670  -18.561 1.00 46.97  ? 398 ARG   A O   1 
ATOM   1667 C  CB  . ARG   A 1 219 ? 12.691 0.168   -17.807 1.00 44.67  ? 398 ARG   A CB  1 
ATOM   1668 C  CG  . ARG   A 1 219 ? 12.446 1.659   -17.985 1.00 45.65  ? 398 ARG   A CG  1 
ATOM   1669 C  CD  . ARG   A 1 219 ? 13.600 2.406   -18.628 1.00 46.45  ? 398 ARG   A CD  1 
ATOM   1670 N  NE  . ARG   A 1 219 ? 13.314 3.830   -18.771 1.00 48.39  ? 398 ARG   A NE  1 
ATOM   1671 C  CZ  . ARG   A 1 219 ? 12.425 4.359   -19.609 1.00 49.66  ? 398 ARG   A CZ  1 
ATOM   1672 N  NH1 . ARG   A 1 219 ? 11.763 3.594   -20.459 1.00 50.40  ? 398 ARG   A NH1 1 
ATOM   1673 N  NH2 . ARG   A 1 219 ? 12.212 5.664   -19.604 1.00 49.72  ? 398 ARG   A NH2 1 
ATOM   1674 N  N   . ALA   A 1 220 ? 11.948 -2.762  -16.328 1.00 47.42  ? 399 ALA   A N   1 
ATOM   1675 C  CA  . ALA   A 1 220 ? 12.152 -4.201  -16.287 1.00 51.07  ? 399 ALA   A CA  1 
ATOM   1676 C  C   . ALA   A 1 220 ? 10.817 -4.925  -16.448 1.00 54.75  ? 399 ALA   A C   1 
ATOM   1677 O  O   . ALA   A 1 220 ? 10.755 -5.975  -17.086 1.00 55.11  ? 399 ALA   A O   1 
ATOM   1678 C  CB  . ALA   A 1 220 ? 12.849 -4.594  -15.007 1.00 49.55  ? 399 ALA   A CB  1 
ATOM   1679 N  N   . LYS   A 1 221 ? 9.756  -4.344  -15.871 1.00 58.04  ? 400 LYS   A N   1 
ATOM   1680 C  CA  . LYS   A 1 221 ? 8.431  -4.946  -15.875 1.00 62.31  ? 400 LYS   A CA  1 
ATOM   1681 C  C   . LYS   A 1 221 ? 7.760  -4.751  -17.234 1.00 64.56  ? 400 LYS   A C   1 
ATOM   1682 O  O   . LYS   A 1 221 ? 7.135  -5.676  -17.751 1.00 65.39  ? 400 LYS   A O   1 
ATOM   1683 C  CB  . LYS   A 1 221 ? 7.571  -4.399  -14.730 1.00 62.49  ? 400 LYS   A CB  1 
ATOM   1684 C  CG  . LYS   A 1 221 ? 7.958  -4.857  -13.327 1.00 63.60  ? 400 LYS   A CG  1 
ATOM   1685 C  CD  . LYS   A 1 221 ? 7.924  -6.365  -13.112 1.00 64.86  ? 400 LYS   A CD  1 
ATOM   1686 C  CE  . LYS   A 1 221 ? 6.560  -6.999  -13.300 1.00 65.19  ? 400 LYS   A CE  1 
ATOM   1687 N  NZ  . LYS   A 1 221 ? 5.579  -6.520  -12.299 1.00 65.86  ? 400 LYS   A NZ  1 
ATOM   1688 N  N   . VAL   A 1 222 ? 7.894  -3.544  -17.799 1.00 67.13  ? 401 VAL   A N   1 
ATOM   1689 C  CA  . VAL   A 1 222 ? 7.275  -3.207  -19.073 1.00 71.42  ? 401 VAL   A CA  1 
ATOM   1690 C  C   . VAL   A 1 222 ? 7.932  -4.024  -20.184 1.00 73.96  ? 401 VAL   A C   1 
ATOM   1691 O  O   . VAL   A 1 222 ? 7.258  -4.796  -20.864 1.00 74.70  ? 401 VAL   A O   1 
ATOM   1692 C  CB  . VAL   A 1 222 ? 7.316  -1.690  -19.358 1.00 71.27  ? 401 VAL   A CB  1 
ATOM   1693 C  CG1 . VAL   A 1 222 ? 6.870  -1.360  -20.775 1.00 70.90  ? 401 VAL   A CG1 1 
ATOM   1694 C  CG2 . VAL   A 1 222 ? 6.496  -0.900  -18.349 1.00 71.28  ? 401 VAL   A CG2 1 
ATOM   1695 N  N   . LYS   A 1 223 ? 9.251  -3.852  -20.350 1.00 76.34  ? 402 LYS   A N   1 
ATOM   1696 C  CA  . LYS   A 1 223 ? 10.004 -4.548  -21.381 1.00 77.28  ? 402 LYS   A CA  1 
ATOM   1697 C  C   . LYS   A 1 223 ? 10.728 -5.744  -20.751 1.00 76.72  ? 402 LYS   A C   1 
ATOM   1698 O  O   . LYS   A 1 223 ? 10.498 -6.869  -21.239 1.00 76.76  ? 402 LYS   A O   1 
ATOM   1699 C  CB  . LYS   A 1 223 ? 10.996 -3.595  -22.058 1.00 77.74  ? 402 LYS   A CB  1 
ATOM   1700 C  CG  . LYS   A 1 223 ? 11.496 -4.037  -23.429 1.00 77.21  ? 402 LYS   A CG  1 
ATOM   1701 C  CD  . LYS   A 1 223 ? 12.593 -3.160  -24.009 1.00 76.08  ? 402 LYS   A CD  1 
ATOM   1702 C  CE  . LYS   A 1 223 ? 13.995 -3.563  -23.598 1.00 75.41  ? 402 LYS   A CE  1 
ATOM   1703 N  NZ  . LYS   A 1 223 ? 14.232 -3.399  -22.144 1.00 75.95  ? 402 LYS   A NZ  1 
HETATM 1704 FE FE  . FE2   B 2 .   ? 25.741 -12.482 -4.908  1.00 38.96  ? 501 FE2   A FE  1 
HETATM 1705 S  S   . SO4   C 3 .   ? 23.821 5.239   22.594  1.00 58.14  ? 502 SO4   A S   1 
HETATM 1706 O  O1  . SO4   C 3 .   ? 24.097 4.577   21.349  1.00 55.47  ? 502 SO4   A O1  1 
HETATM 1707 O  O2  . SO4   C 3 .   ? 23.878 6.662   22.404  1.00 57.66  ? 502 SO4   A O2  1 
HETATM 1708 O  O3  . SO4   C 3 .   ? 24.800 4.850   23.575  1.00 58.41  ? 502 SO4   A O3  1 
HETATM 1709 O  O4  . SO4   C 3 .   ? 22.510 4.867   23.050  1.00 58.36  ? 502 SO4   A O4  1 
HETATM 1710 S  S   . SO4   D 3 .   ? 33.116 7.137   32.702  1.00 97.39  ? 503 SO4   A S   1 
HETATM 1711 O  O1  . SO4   D 3 .   ? 34.051 7.785   31.823  1.00 94.83  ? 503 SO4   A O1  1 
HETATM 1712 O  O2  . SO4   D 3 .   ? 31.972 6.709   31.944  1.00 101.28 ? 503 SO4   A O2  1 
HETATM 1713 O  O3  . SO4   D 3 .   ? 33.737 5.994   33.316  1.00 94.10  ? 503 SO4   A O3  1 
HETATM 1714 O  O4  . SO4   D 3 .   ? 32.699 8.060   33.723  1.00 99.01  ? 503 SO4   A O4  1 
HETATM 1715 CL CL  . CL    E 4 .   ? 38.926 7.305   0.645   1.00 62.28  ? 504 CL    A CL  1 
HETATM 1716 C  C1  . A1L0X F 5 .   ? 23.423 -16.250 -3.264  1.00 45.12  ? 505 A1L0X A C1  1 
HETATM 1717 C  C2  . A1L0X F 5 .   ? 23.694 -14.851 -5.072  1.00 46.59  ? 505 A1L0X A C2  1 
HETATM 1718 C  C3  . A1L0X F 5 .   ? 25.080 -14.577 -3.258  1.00 42.45  ? 505 A1L0X A C3  1 
HETATM 1719 C  C7  . A1L0X F 5 .   ? 27.512 -13.291 -0.674  1.00 37.50  ? 505 A1L0X A C7  1 
HETATM 1720 C  C6  . A1L0X F 5 .   ? 26.232 -13.821 -2.667  1.00 40.46  ? 505 A1L0X A C6  1 
HETATM 1721 O  O2  . A1L0X F 5 .   ? 26.851 -13.037 -3.378  1.00 38.63  ? 505 A1L0X A O2  1 
HETATM 1722 C  C4  . A1L0X F 5 .   ? 24.452 -15.613 -2.621  1.00 44.58  ? 505 A1L0X A C4  1 
HETATM 1723 C  C5  . A1L0X F 5 .   ? 23.261 -14.445 -6.454  1.00 48.04  ? 505 A1L0X A C5  1 
HETATM 1724 O  O3  . A1L0X F 5 .   ? 28.587 -13.014 1.407   1.00 33.79  ? 505 A1L0X A O3  1 
HETATM 1725 C  C11 . A1L0X F 5 .   ? 20.908 -14.083 -5.587  1.00 49.68  ? 505 A1L0X A C11 1 
HETATM 1726 C  C13 . A1L0X F 5 .   ? 19.217 -12.930 -6.879  1.00 49.95  ? 505 A1L0X A C13 1 
HETATM 1727 C  C15 . A1L0X F 5 .   ? 21.457 -13.247 -7.747  1.00 50.37  ? 505 A1L0X A C15 1 
HETATM 1728 N  N1  . A1L0X F 5 .   ? 23.044 -15.871 -4.494  1.00 46.02  ? 505 A1L0X A N1  1 
HETATM 1729 C  C18 . A1L0X F 5 .   ? 15.833 -12.049 -8.337  1.00 49.30  ? 505 A1L0X A C18 1 
HETATM 1730 C  C10 . A1L0X F 5 .   ? 21.852 -13.916 -6.596  1.00 49.64  ? 505 A1L0X A C10 1 
HETATM 1731 C  C12 . A1L0X F 5 .   ? 19.616 -13.601 -5.724  1.00 50.07  ? 505 A1L0X A C12 1 
HETATM 1732 C  C14 . A1L0X F 5 .   ? 20.167 -12.759 -7.888  1.00 49.31  ? 505 A1L0X A C14 1 
HETATM 1733 C  C16 . A1L0X F 5 .   ? 17.835 -12.397 -7.022  1.00 49.61  ? 505 A1L0X A C16 1 
HETATM 1734 C  C17 . A1L0X F 5 .   ? 17.116 -12.561 -8.206  1.00 49.14  ? 505 A1L0X A C17 1 
HETATM 1735 C  C19 . A1L0X F 5 .   ? 15.247 -11.366 -7.294  1.00 49.37  ? 505 A1L0X A C19 1 
HETATM 1736 O  O1  . A1L0X F 5 .   ? 24.775 -16.060 -1.376  1.00 46.48  ? 505 A1L0X A O1  1 
HETATM 1737 N  N2  . A1L0X F 5 .   ? 24.705 -14.182 -4.517  1.00 43.03  ? 505 A1L0X A N2  1 
HETATM 1738 C  C8  . A1L0X F 5 .   ? 27.664 -13.607 0.808   1.00 35.75  ? 505 A1L0X A C8  1 
HETATM 1739 C  C9  . A1L0X F 5 .   ? 22.684 -17.386 -2.629  1.00 45.66  ? 505 A1L0X A C9  1 
HETATM 1740 O  O4  . A1L0X F 5 .   ? 26.877 -14.430 1.325   1.00 34.57  ? 505 A1L0X A O4  1 
HETATM 1741 N  N3  . A1L0X F 5 .   ? 26.506 -14.055 -1.381  1.00 40.27  ? 505 A1L0X A N3  1 
HETATM 1742 C  C20 . A1L0X F 5 .   ? 15.941 -11.190 -6.115  1.00 50.20  ? 505 A1L0X A C20 1 
HETATM 1743 C  C21 . A1L0X F 5 .   ? 17.226 -11.698 -5.981  1.00 49.96  ? 505 A1L0X A C21 1 
HETATM 1744 O  O   . HOH   G 6 .   ? 28.341 16.006  10.334  1.00 49.55  ? 601 HOH   A O   1 
HETATM 1745 O  O   . HOH   G 6 .   ? 31.759 -6.740  -14.774 1.00 38.87  ? 602 HOH   A O   1 
HETATM 1746 O  O   . HOH   G 6 .   ? 35.020 -3.528  -18.096 1.00 40.93  ? 603 HOH   A O   1 
HETATM 1747 O  O   . HOH   G 6 .   ? 30.015 -1.105  -15.894 1.00 46.53  ? 604 HOH   A O   1 
HETATM 1748 O  O   . HOH   G 6 .   ? 12.710 -21.922 1.549   1.00 36.47  ? 605 HOH   A O   1 
HETATM 1749 O  O   . HOH   G 6 .   ? 28.470 -5.693  17.426  1.00 38.89  ? 606 HOH   A O   1 
HETATM 1750 O  O   . HOH   G 6 .   ? 10.588 -22.190 11.508  1.00 45.41  ? 607 HOH   A O   1 
HETATM 1751 O  O   . HOH   G 6 .   ? 27.395 12.483  1.892   1.00 48.07  ? 608 HOH   A O   1 
HETATM 1752 O  O   . HOH   G 6 .   ? 39.815 -15.566 -5.920  1.00 47.87  ? 609 HOH   A O   1 
HETATM 1753 O  O   . HOH   G 6 .   ? 24.254 -14.764 0.823   1.00 36.92  ? 610 HOH   A O   1 
HETATM 1754 O  O   . HOH   G 6 .   ? 23.149 -0.910  -14.087 1.00 51.14  ? 611 HOH   A O   1 
HETATM 1755 O  O   . HOH   G 6 .   ? 16.025 -11.292 -12.403 1.00 52.72  ? 612 HOH   A O   1 
HETATM 1756 O  O   . HOH   G 6 .   ? 22.237 -13.817 2.182   1.00 31.69  ? 613 HOH   A O   1 
HETATM 1757 O  O   . HOH   G 6 .   ? 17.893 -21.231 17.408  1.00 46.19  ? 614 HOH   A O   1 
HETATM 1758 O  O   . HOH   G 6 .   ? 37.921 -20.461 1.587   1.00 43.85  ? 615 HOH   A O   1 
HETATM 1759 O  O   . HOH   G 6 .   ? 7.106  -18.699 11.287  1.00 57.70  ? 616 HOH   A O   1 
HETATM 1760 O  O   . HOH   G 6 .   ? 26.990 0.444   -13.997 1.00 47.60  ? 617 HOH   A O   1 
HETATM 1761 O  O   . HOH   G 6 .   ? 16.968 -23.726 16.729  1.00 49.32  ? 618 HOH   A O   1 
HETATM 1762 O  O   . HOH   G 6 .   ? 20.169 -24.435 17.009  1.00 61.85  ? 619 HOH   A O   1 
HETATM 1763 O  O   . HOH   G 6 .   ? 35.973 -7.160  -12.139 1.00 35.16  ? 620 HOH   A O   1 
HETATM 1764 O  O   . HOH   G 6 .   ? 13.108 -18.279 13.443  1.00 39.81  ? 621 HOH   A O   1 
HETATM 1765 O  O   . HOH   G 6 .   ? 10.474 -5.120  8.834   1.00 55.67  ? 622 HOH   A O   1 
HETATM 1766 O  O   . HOH   G 6 .   ? 19.752 12.544  3.055   1.00 57.73  ? 623 HOH   A O   1 
HETATM 1767 O  O   . HOH   G 6 .   ? 30.774 -6.357  13.028  1.00 33.22  ? 624 HOH   A O   1 
HETATM 1768 O  O   . HOH   G 6 .   ? 12.573 4.706   -16.302 1.00 63.29  ? 625 HOH   A O   1 
HETATM 1769 O  O   . HOH   G 6 .   ? 22.085 -5.001  -14.838 1.00 36.27  ? 626 HOH   A O   1 
HETATM 1770 O  O   . HOH   G 6 .   ? 9.666  -7.611  3.448   1.00 35.29  ? 627 HOH   A O   1 
HETATM 1771 O  O   . HOH   G 6 .   ? 19.441 -9.366  -13.958 1.00 41.73  ? 628 HOH   A O   1 
HETATM 1772 O  O   . HOH   G 6 .   ? 33.376 0.012   -11.482 1.00 41.23  ? 629 HOH   A O   1 
HETATM 1773 O  O   . HOH   G 6 .   ? 14.114 -10.001 -10.957 1.00 61.14  ? 630 HOH   A O   1 
HETATM 1774 O  O   . HOH   G 6 .   ? 26.894 -7.801  -8.375  1.00 32.98  ? 631 HOH   A O   1 
HETATM 1775 O  O   . HOH   G 6 .   ? 39.696 -20.731 -2.597  1.00 66.82  ? 632 HOH   A O   1 
HETATM 1776 O  O   . HOH   G 6 .   ? 17.538 4.667   -13.551 1.00 58.78  ? 633 HOH   A O   1 
HETATM 1777 O  O   . HOH   G 6 .   ? 24.856 -11.106 -3.299  1.00 27.34  ? 634 HOH   A O   1 
HETATM 1778 O  O   . HOH   G 6 .   ? 32.403 -1.168  -6.941  1.00 32.49  ? 635 HOH   A O   1 
HETATM 1779 O  O   . HOH   G 6 .   ? 39.033 -9.775  -12.267 1.00 48.96  ? 636 HOH   A O   1 
HETATM 1780 O  O   . HOH   G 6 .   ? 23.768 -1.460  -9.452  1.00 35.46  ? 637 HOH   A O   1 
HETATM 1781 O  O   . HOH   G 6 .   ? 33.703 0.374   3.729   1.00 37.15  ? 638 HOH   A O   1 
HETATM 1782 O  O   . HOH   G 6 .   ? 35.514 -19.650 12.611  1.00 43.95  ? 639 HOH   A O   1 
HETATM 1783 O  O   . HOH   G 6 .   ? 38.618 -5.646  -9.100  1.00 26.86  ? 640 HOH   A O   1 
HETATM 1784 O  O   . HOH   G 6 .   ? 21.940 -5.411  20.349  1.00 46.69  ? 641 HOH   A O   1 
HETATM 1785 O  O   . HOH   G 6 .   ? 30.905 3.515   -7.400  1.00 53.76  ? 642 HOH   A O   1 
HETATM 1786 O  O   . HOH   G 6 .   ? 11.622 -19.320 1.368   1.00 38.75  ? 643 HOH   A O   1 
HETATM 1787 O  O   . HOH   G 6 .   ? 37.038 -8.550  5.901   1.00 37.70  ? 644 HOH   A O   1 
HETATM 1788 O  O   . HOH   G 6 .   ? 23.759 -12.369 -1.209  1.00 32.00  ? 645 HOH   A O   1 
HETATM 1789 O  O   . HOH   G 6 .   ? 34.720 -30.824 5.770   1.00 76.37  ? 646 HOH   A O   1 
HETATM 1790 O  O   . HOH   G 6 .   ? 26.896 -13.389 -13.350 1.00 44.06  ? 647 HOH   A O   1 
HETATM 1791 O  O   . HOH   G 6 .   ? 17.605 3.191   12.151  1.00 55.93  ? 648 HOH   A O   1 
HETATM 1792 O  O   . HOH   G 6 .   ? 19.007 5.959   13.654  1.00 45.05  ? 649 HOH   A O   1 
HETATM 1793 O  O   . HOH   G 6 .   ? 30.436 -18.581 13.298  1.00 46.77  ? 650 HOH   A O   1 
HETATM 1794 O  O   . HOH   G 6 .   ? 33.792 -11.018 -13.870 1.00 51.92  ? 651 HOH   A O   1 
HETATM 1795 O  O   . HOH   G 6 .   ? 29.145 11.237  -2.653  1.00 43.13  ? 652 HOH   A O   1 
HETATM 1796 O  O   . HOH   G 6 .   ? 9.947  -5.857  6.372   1.00 56.67  ? 653 HOH   A O   1 
HETATM 1797 O  O   . HOH   G 6 .   ? 42.113 -11.516 3.023   1.00 43.21  ? 654 HOH   A O   1 
HETATM 1798 O  O   . HOH   G 6 .   ? 40.220 -7.782  3.862   1.00 38.01  ? 655 HOH   A O   1 
HETATM 1799 O  O   . HOH   G 6 .   ? 13.665 0.435   12.557  1.00 55.58  ? 656 HOH   A O   1 
HETATM 1800 O  O   . HOH   G 6 .   ? 18.752 9.292   11.653  1.00 35.50  ? 657 HOH   A O   1 
HETATM 1801 O  O   . HOH   G 6 .   ? 29.346 -25.033 -3.405  1.00 55.83  ? 658 HOH   A O   1 
HETATM 1802 O  O   . HOH   G 6 .   ? 27.012 -18.782 12.515  1.00 49.65  ? 659 HOH   A O   1 
HETATM 1803 O  O   . HOH   G 6 .   ? 36.328 -0.402  -4.756  1.00 36.18  ? 660 HOH   A O   1 
HETATM 1804 O  O   . HOH   G 6 .   ? 22.621 -13.714 -10.970 1.00 59.30  ? 661 HOH   A O   1 
HETATM 1805 O  O   . HOH   G 6 .   ? 26.847 -17.675 14.981  1.00 49.29  ? 662 HOH   A O   1 
HETATM 1806 O  O   . HOH   G 6 .   ? 40.636 1.779   -1.494  1.00 59.60  ? 663 HOH   A O   1 
HETATM 1807 O  O   . HOH   G 6 .   ? 31.884 -12.336 17.206  1.00 48.79  ? 664 HOH   A O   1 
HETATM 1808 O  O   . HOH   G 6 .   ? 38.245 -5.478  -13.117 1.00 45.78  ? 665 HOH   A O   1 
HETATM 1809 O  O   . HOH   G 6 .   ? 23.584 5.714   -10.785 1.00 49.14  ? 666 HOH   A O   1 
HETATM 1810 O  O   . HOH   G 6 .   ? 16.433 -25.875 6.439   1.00 41.30  ? 667 HOH   A O   1 
HETATM 1811 O  O   . HOH   G 6 .   ? 32.900 -12.737 13.679  1.00 39.67  ? 668 HOH   A O   1 
HETATM 1812 O  O   . HOH   G 6 .   ? 27.632 6.712   -8.186  1.00 56.01  ? 669 HOH   A O   1 
HETATM 1813 O  O   . HOH   G 6 .   ? 36.505 -0.009  24.297  1.00 53.66  ? 670 HOH   A O   1 
HETATM 1814 O  O   . HOH   G 6 .   ? 37.858 -17.698 2.458   1.00 35.08  ? 671 HOH   A O   1 
HETATM 1815 O  O   . HOH   G 6 .   ? 10.649 -1.298  2.537   1.00 58.07  ? 672 HOH   A O   1 
HETATM 1816 O  O   . HOH   G 6 .   ? 34.186 7.656   2.334   1.00 62.12  ? 673 HOH   A O   1 
HETATM 1817 O  O   . HOH   G 6 .   ? 23.941 -16.285 -10.125 1.00 56.43  ? 674 HOH   A O   1 
HETATM 1818 O  O   . HOH   G 6 .   ? 19.981 -12.686 -11.652 1.00 61.43  ? 675 HOH   A O   1 
HETATM 1819 O  O   . HOH   G 6 .   ? 34.574 -20.045 -4.850  1.00 58.19  ? 676 HOH   A O   1 
HETATM 1820 O  O   . HOH   G 6 .   ? 17.695 12.140  4.792   1.00 48.35  ? 677 HOH   A O   1 
HETATM 1821 O  O   . HOH   G 6 .   ? 10.682 -3.728  12.616  1.00 58.53  ? 678 HOH   A O   1 
HETATM 1822 O  O   . HOH   G 6 .   ? 13.623 9.067   1.361   1.00 56.00  ? 679 HOH   A O   1 
HETATM 1823 O  O   . HOH   G 6 .   ? 9.084  -2.745  -1.393  1.00 48.34  ? 680 HOH   A O   1 
HETATM 1824 O  O   . HOH   G 6 .   ? 21.620 6.746   18.081  1.00 54.82  ? 681 HOH   A O   1 
HETATM 1825 O  O   . HOH   G 6 .   ? 27.681 -2.346  24.158  1.00 55.09  ? 682 HOH   A O   1 
HETATM 1826 O  O   . HOH   G 6 .   ? 24.948 -26.708 8.363   1.00 49.60  ? 683 HOH   A O   1 
HETATM 1827 O  O   . HOH   G 6 .   ? 11.357 -11.079 -2.931  1.00 42.28  ? 684 HOH   A O   1 
HETATM 1828 O  O   . HOH   G 6 .   ? 30.017 -25.091 12.270  1.00 51.74  ? 685 HOH   A O   1 
HETATM 1829 O  O   . HOH   G 6 .   ? 8.959  -7.174  -0.674  1.00 63.63  ? 686 HOH   A O   1 
HETATM 1830 O  O   . HOH   G 6 .   ? 24.629 -23.227 13.290  1.00 58.96  ? 687 HOH   A O   1 
HETATM 1831 O  O   . HOH   G 6 .   ? 39.902 -28.083 3.036   1.00 66.89  ? 688 HOH   A O   1 
HETATM 1832 O  O   . HOH   G 6 .   ? 40.765 -20.995 4.564   1.00 58.48  ? 689 HOH   A O   1 
HETATM 1833 O  O   . HOH   G 6 .   ? 12.583 -8.281  18.323  1.00 67.75  ? 690 HOH   A O   1 
HETATM 1834 O  O   . HOH   G 6 .   ? 24.158 -4.951  22.736  1.00 49.72  ? 691 HOH   A O   1 
HETATM 1835 O  O   . HOH   G 6 .   ? 30.939 3.524   34.713  1.00 56.28  ? 692 HOH   A O   1 
HETATM 1836 O  O   . HOH   G 6 .   ? 26.559 3.160   -13.838 1.00 63.49  ? 693 HOH   A O   1 
HETATM 1837 O  O   . HOH   G 6 .   ? 38.500 -12.340 -14.391 1.00 69.27  ? 694 HOH   A O   1 
HETATM 1838 O  O   . HOH   G 6 .   ? 41.048 -17.903 -4.973  1.00 60.65  ? 695 HOH   A O   1 
HETATM 1839 O  O   . HOH   G 6 .   ? 12.173 0.959   0.328   1.00 55.74  ? 696 HOH   A O   1 
HETATM 1840 O  O   . HOH   G 6 .   ? 33.117 -20.844 13.129  1.00 54.14  ? 697 HOH   A O   1 
HETATM 1841 O  O   . HOH   G 6 .   ? 17.812 -27.747 4.487   1.00 55.08  ? 698 HOH   A O   1 
HETATM 1842 O  O   . HOH   G 6 .   ? 10.038 4.381   -16.155 1.00 59.04  ? 699 HOH   A O   1 
HETATM 1843 O  O   . HOH   G 6 .   ? 30.099 -8.615  -15.803 1.00 48.90  ? 700 HOH   A O   1 
HETATM 1844 O  O   . HOH   G 6 .   ? 36.036 2.302   2.226   1.00 66.31  ? 701 HOH   A O   1 
HETATM 1845 O  O   . HOH   G 6 .   ? 32.326 0.511   -9.022  1.00 39.73  ? 702 HOH   A O   1 
HETATM 1846 O  O   . HOH   G 6 .   ? 39.429 -7.116  -11.276 1.00 48.12  ? 703 HOH   A O   1 
HETATM 1847 O  O   . HOH   G 6 .   ? 31.062 -12.497 -13.483 1.00 50.12  ? 704 HOH   A O   1 
HETATM 1848 O  O   . HOH   G 6 .   ? 28.681 12.713  -0.498  1.00 46.89  ? 705 HOH   A O   1 
HETATM 1849 O  O   . HOH   G 6 .   ? 36.990 -28.772 7.422   1.00 71.84  ? 706 HOH   A O   1 
HETATM 1850 O  O   . HOH   G 6 .   ? 34.431 -7.089  -14.386 1.00 43.29  ? 707 HOH   A O   1 
HETATM 1851 O  O   . HOH   G 6 .   ? 27.171 -11.753 -15.451 1.00 50.10  ? 708 HOH   A O   1 
HETATM 1852 O  O   . HOH   G 6 .   ? 13.640 2.929   0.788   1.00 61.76  ? 709 HOH   A O   1 
HETATM 1853 O  O   . HOH   G 6 .   ? 31.528 13.224  2.017   1.00 55.43  ? 710 HOH   A O   1 
HETATM 1854 O  O   . HOH   G 6 .   ? 40.054 -27.081 5.710   1.00 65.20  ? 711 HOH   A O   1 
HETATM 1855 O  O   . HOH   G 6 .   ? 17.497 -16.050 -5.963  1.00 63.49  ? 712 HOH   A O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . HIS A 3   ? 0.4444 0.5742 0.2938 -0.0912 -0.0347 -0.0275 182 HIS A N   
2    C CA  . HIS A 3   ? 0.4472 0.5803 0.2928 -0.0970 -0.0387 -0.0364 182 HIS A CA  
3    C C   . HIS A 3   ? 0.4203 0.5476 0.2704 -0.0952 -0.0296 -0.0543 182 HIS A C   
4    O O   . HIS A 3   ? 0.4039 0.5212 0.2706 -0.0863 -0.0255 -0.0566 182 HIS A O   
5    C CB  . HIS A 3   ? 0.4811 0.6131 0.3398 -0.0943 -0.0484 -0.0279 182 HIS A CB  
6    C CG  . HIS A 3   ? 0.4987 0.6381 0.3504 -0.1030 -0.0555 -0.0329 182 HIS A CG  
7    N ND1 . HIS A 3   ? 0.5286 0.6796 0.3599 -0.1134 -0.0606 -0.0321 182 HIS A ND1 
8    C CD2 . HIS A 3   ? 0.5154 0.6530 0.3773 -0.1037 -0.0585 -0.0386 182 HIS A CD2 
9    C CE1 . HIS A 3   ? 0.5222 0.6788 0.3519 -0.1200 -0.0668 -0.0377 182 HIS A CE1 
10   N NE2 . HIS A 3   ? 0.5054 0.6538 0.3541 -0.1144 -0.0656 -0.0417 182 HIS A NE2 
11   N N   . HIS A 4   ? 0.3929 0.5266 0.2275 -0.1039 -0.0269 -0.0667 183 HIS A N   
12   C CA  . HIS A 4   ? 0.3857 0.5152 0.2211 -0.1028 -0.0169 -0.0851 183 HIS A CA  
13   C C   . HIS A 4   ? 0.3746 0.4928 0.2230 -0.1000 -0.0181 -0.0936 183 HIS A C   
14   O O   . HIS A 4   ? 0.3808 0.4922 0.2319 -0.0981 -0.0108 -0.1090 183 HIS A O   
15   C CB  . HIS A 4   ? 0.3863 0.5274 0.1995 -0.1140 -0.0136 -0.0959 183 HIS A CB  
16   C CG  . HIS A 4   ? 0.3928 0.5400 0.1933 -0.1247 -0.0221 -0.0977 183 HIS A CG  
17   N ND1 . HIS A 4   ? 0.3975 0.5572 0.1802 -0.1340 -0.0300 -0.0870 183 HIS A ND1 
18   C CD2 . HIS A 4   ? 0.3919 0.5345 0.1949 -0.1280 -0.0245 -0.1084 183 HIS A CD2 
19   C CE1 . HIS A 4   ? 0.3928 0.5571 0.1679 -0.1425 -0.0373 -0.0914 183 HIS A CE1 
20   N NE2 . HIS A 4   ? 0.3975 0.5515 0.1848 -0.1394 -0.0338 -0.1048 183 HIS A NE2 
21   N N   . HIS A 5   ? 0.3504 0.4666 0.2070 -0.0999 -0.0272 -0.0837 184 HIS A N   
22   C CA  . HIS A 5   ? 0.3387 0.4443 0.2075 -0.0988 -0.0287 -0.0900 184 HIS A CA  
23   C C   . HIS A 5   ? 0.3307 0.4231 0.2189 -0.0870 -0.0247 -0.0863 184 HIS A C   
24   O O   . HIS A 5   ? 0.3171 0.3978 0.2156 -0.0852 -0.0240 -0.0918 184 HIS A O   
25   C CB  . HIS A 5   ? 0.3221 0.4343 0.1912 -0.1054 -0.0398 -0.0824 184 HIS A CB  
26   C CG  . HIS A 5   ? 0.3149 0.4394 0.1651 -0.1179 -0.0447 -0.0878 184 HIS A CG  
27   N ND1 . HIS A 5   ? 0.3083 0.4470 0.1501 -0.1232 -0.0546 -0.0753 184 HIS A ND1 
28   C CD2 . HIS A 5   ? 0.3189 0.4438 0.1567 -0.1262 -0.0416 -0.1042 184 HIS A CD2 
29   C CE1 . HIS A 5   ? 0.3087 0.4570 0.1325 -0.1349 -0.0577 -0.0834 184 HIS A CE1 
30   N NE2 . HIS A 5   ? 0.3139 0.4542 0.1347 -0.1372 -0.0495 -0.1016 184 HIS A NE2 
31   N N   . HIS A 6   ? 0.3346 0.4286 0.2266 -0.0800 -0.0222 -0.0769 185 HIS A N   
32   C CA  . HIS A 6   ? 0.3454 0.4290 0.2538 -0.0694 -0.0189 -0.0723 185 HIS A CA  
33   C C   . HIS A 6   ? 0.3504 0.4298 0.2605 -0.0634 -0.0095 -0.0818 185 HIS A C   
34   O O   . HIS A 6   ? 0.3438 0.4320 0.2429 -0.0665 -0.0053 -0.0869 185 HIS A O   
35   C CB  . HIS A 6   ? 0.3534 0.4413 0.2669 -0.0655 -0.0229 -0.0560 185 HIS A CB  
36   C CG  . HIS A 6   ? 0.3573 0.4499 0.2734 -0.0690 -0.0321 -0.0466 185 HIS A CG  
37   N ND1 . HIS A 6   ? 0.3560 0.4437 0.2874 -0.0643 -0.0346 -0.0400 185 HIS A ND1 
38   C CD2 . HIS A 6   ? 0.3575 0.4608 0.2638 -0.0767 -0.0394 -0.0428 185 HIS A CD2 
39   C CE1 . HIS A 6   ? 0.3578 0.4539 0.2901 -0.0685 -0.0428 -0.0331 185 HIS A CE1 
40   N NE2 . HIS A 6   ? 0.3545 0.4599 0.2719 -0.0758 -0.0464 -0.0342 185 HIS A NE2 
41   N N   . HIS A 7   ? 0.3479 0.4149 0.2722 -0.0551 -0.0066 -0.0836 186 HIS A N   
42   C CA  . HIS A 7   ? 0.3541 0.4169 0.2838 -0.0478 0.0013  -0.0925 186 HIS A CA  
43   C C   . HIS A 7   ? 0.3370 0.3920 0.2813 -0.0379 0.0017  -0.0840 186 HIS A C   
44   O O   . HIS A 7   ? 0.3103 0.3573 0.2621 -0.0367 -0.0026 -0.0769 186 HIS A O   
45   C CB  . HIS A 7   ? 0.3739 0.4272 0.3034 -0.0487 0.0046  -0.1086 186 HIS A CB  
46   C CG  . HIS A 7   ? 0.4052 0.4661 0.3191 -0.0597 0.0037  -0.1173 186 HIS A CG  
47   N ND1 . HIS A 7   ? 0.4122 0.4877 0.3126 -0.0646 0.0075  -0.1220 186 HIS A ND1 
48   C CD2 . HIS A 7   ? 0.4206 0.4780 0.3294 -0.0679 -0.0007 -0.1220 186 HIS A CD2 
49   C CE1 . HIS A 7   ? 0.4120 0.4921 0.2985 -0.0752 0.0052  -0.1293 186 HIS A CE1 
50   N NE2 . HIS A 7   ? 0.4196 0.4891 0.3114 -0.0772 -0.0001 -0.1296 186 HIS A NE2 
51   N N   . HIS A 8   ? 0.3371 0.3963 0.2852 -0.0315 0.0069  -0.0850 187 HIS A N   
52   C CA  . HIS A 8   ? 0.3428 0.3969 0.3033 -0.0227 0.0072  -0.0774 187 HIS A CA  
53   C C   . HIS A 8   ? 0.3224 0.3611 0.2938 -0.0162 0.0078  -0.0826 187 HIS A C   
54   O O   . HIS A 8   ? 0.3085 0.3426 0.2806 -0.0145 0.0115  -0.0950 187 HIS A O   
55   C CB  . HIS A 8   ? 0.3777 0.4427 0.3392 -0.0190 0.0121  -0.0772 187 HIS A CB  
56   C CG  . HIS A 8   ? 0.4044 0.4777 0.3608 -0.0226 0.0096  -0.0653 187 HIS A CG  
57   N ND1 . HIS A 8   ? 0.4233 0.4923 0.3868 -0.0189 0.0062  -0.0540 187 HIS A ND1 
58   C CD2 . HIS A 8   ? 0.4263 0.5107 0.3712 -0.0295 0.0100  -0.0628 187 HIS A CD2 
59   C CE1 . HIS A 8   ? 0.4320 0.5081 0.3894 -0.0229 0.0047  -0.0456 187 HIS A CE1 
60   N NE2 . HIS A 8   ? 0.4439 0.5288 0.3898 -0.0294 0.0066  -0.0500 187 HIS A NE2 
61   N N   . LEU A 9   ? 0.3148 0.3449 0.2940 -0.0129 0.0042  -0.0728 188 LEU A N   
62   C CA  . LEU A 9   ? 0.3167 0.3320 0.3062 -0.0057 0.0044  -0.0739 188 LEU A CA  
63   C C   . LEU A 9   ? 0.2994 0.3188 0.2960 0.0035  0.0083  -0.0760 188 LEU A C   
64   O O   . LEU A 9   ? 0.2848 0.3151 0.2816 0.0047  0.0087  -0.0693 188 LEU A O   
65   C CB  . LEU A 9   ? 0.3286 0.3375 0.3226 -0.0059 0.0000  -0.0616 188 LEU A CB  
66   C CG  . LEU A 9   ? 0.3363 0.3401 0.3274 -0.0141 -0.0039 -0.0597 188 LEU A CG  
67   C CD1 . LEU A 9   ? 0.3495 0.3517 0.3456 -0.0142 -0.0069 -0.0475 188 LEU A CD1 
68   C CD2 . LEU A 9   ? 0.3468 0.3348 0.3393 -0.0152 -0.0034 -0.0688 188 LEU A CD2 
69   N N   . PRO A 10  ? 0.2941 0.3054 0.2975 0.0102  0.0110  -0.0856 189 PRO A N   
70   C CA  . PRO A 10  ? 0.2818 0.2976 0.2952 0.0202  0.0135  -0.0865 189 PRO A CA  
71   C C   . PRO A 10  ? 0.2782 0.2898 0.2975 0.0245  0.0094  -0.0732 189 PRO A C   
72   O O   . PRO A 10  ? 0.2848 0.2851 0.3029 0.0217  0.0054  -0.0656 189 PRO A O   
73   C CB  . PRO A 10  ? 0.2829 0.2855 0.3040 0.0270  0.0154  -0.0980 189 PRO A CB  
74   C CG  . PRO A 10  ? 0.2932 0.2910 0.3048 0.0184  0.0165  -0.1075 189 PRO A CG  
75   C CD  . PRO A 10  ? 0.2946 0.2926 0.2973 0.0087  0.0118  -0.0966 189 PRO A CD  
76   N N   . ALA A 11  ? 0.2778 0.3000 0.3033 0.0307  0.0106  -0.0709 190 ALA A N   
77   C CA  . ALA A 11  ? 0.2810 0.3025 0.3110 0.0344  0.0071  -0.0593 190 ALA A CA  
78   C C   . ALA A 11  ? 0.2862 0.2886 0.3212 0.0389  0.0030  -0.0549 190 ALA A C   
79   O O   . ALA A 11  ? 0.2856 0.2826 0.3182 0.0364  -0.0003 -0.0444 190 ALA A O   
80   C CB  . ALA A 11  ? 0.2755 0.3114 0.3128 0.0407  0.0091  -0.0607 190 ALA A CB  
81   N N   . LEU A 12  ? 0.2770 0.2688 0.3186 0.0452  0.0037  -0.0630 191 LEU A N   
82   C CA  . LEU A 12  ? 0.2847 0.2559 0.3310 0.0498  -0.0004 -0.0585 191 LEU A CA  
83   C C   . LEU A 12  ? 0.2899 0.2481 0.3282 0.0404  -0.0025 -0.0536 191 LEU A C   
84   O O   . LEU A 12  ? 0.2894 0.2369 0.3274 0.0397  -0.0062 -0.0433 191 LEU A O   
85   C CB  . LEU A 12  ? 0.2887 0.2497 0.3438 0.0581  0.0011  -0.0699 191 LEU A CB  
86   C CG  . LEU A 12  ? 0.3001 0.2357 0.3597 0.0626  -0.0033 -0.0657 191 LEU A CG  
87   C CD1 . LEU A 12  ? 0.3064 0.2411 0.3727 0.0709  -0.0082 -0.0541 191 LEU A CD1 
88   C CD2 . LEU A 12  ? 0.3051 0.2277 0.3719 0.0688  -0.0010 -0.0795 191 LEU A CD2 
89   N N   . LYS A 13  ? 0.2935 0.2541 0.3251 0.0325  -0.0001 -0.0611 192 LYS A N   
90   C CA  . LYS A 13  ? 0.3088 0.2595 0.3341 0.0230  -0.0020 -0.0587 192 LYS A CA  
91   C C   . LYS A 13  ? 0.3167 0.2761 0.3380 0.0175  -0.0041 -0.0465 192 LYS A C   
92   O O   . LYS A 13  ? 0.3119 0.2616 0.3327 0.0136  -0.0066 -0.0390 192 LYS A O   
93   C CB  . LYS A 13  ? 0.3071 0.2618 0.3262 0.0162  0.0006  -0.0705 192 LYS A CB  
94   C CG  . LYS A 13  ? 0.3292 0.2717 0.3437 0.0068  -0.0015 -0.0719 192 LYS A CG  
95   C CD  . LYS A 13  ? 0.3441 0.2889 0.3526 0.0013  0.0010  -0.0859 192 LYS A CD  
96   C CE  . LYS A 13  ? 0.3380 0.2729 0.3417 -0.0094 -0.0015 -0.0881 192 LYS A CE  
97   N NZ  . LYS A 13  ? 0.3524 0.2625 0.3616 -0.0077 -0.0027 -0.0888 192 LYS A NZ  
98   N N   . LEU A 14  ? 0.3287 0.3063 0.3476 0.0170  -0.0027 -0.0450 193 LEU A N   
99   C CA  . LEU A 14  ? 0.3374 0.3233 0.3533 0.0128  -0.0041 -0.0349 193 LEU A CA  
100  C C   . LEU A 14  ? 0.3421 0.3225 0.3620 0.0171  -0.0060 -0.0253 193 LEU A C   
101  O O   . LEU A 14  ? 0.3405 0.3185 0.3589 0.0127  -0.0075 -0.0177 193 LEU A O   
102  C CB  . LEU A 14  ? 0.3455 0.3491 0.3582 0.0121  -0.0022 -0.0357 193 LEU A CB  
103  C CG  . LEU A 14  ? 0.3574 0.3693 0.3676 0.0085  -0.0034 -0.0265 193 LEU A CG  
104  C CD1 . LEU A 14  ? 0.3561 0.3667 0.3635 0.0010  -0.0056 -0.0242 193 LEU A CD1 
105  C CD2 . LEU A 14  ? 0.3579 0.3840 0.3649 0.0081  -0.0015 -0.0272 193 LEU A CD2 
106  N N   . ALA A 15  ? 0.3279 0.3074 0.3529 0.0256  -0.0060 -0.0262 194 ALA A N   
107  C CA  . ALA A 15  ? 0.3358 0.3112 0.3633 0.0299  -0.0085 -0.0171 194 ALA A CA  
108  C C   . ALA A 15  ? 0.3476 0.3046 0.3744 0.0275  -0.0111 -0.0117 194 ALA A C   
109  O O   . ALA A 15  ? 0.3395 0.2954 0.3632 0.0238  -0.0123 -0.0026 194 ALA A O   
110  C CB  . ALA A 15  ? 0.3424 0.3211 0.3769 0.0397  -0.0089 -0.0199 194 ALA A CB  
111  N N   . LEU A 16  ? 0.3468 0.2891 0.3760 0.0289  -0.0114 -0.0179 195 LEU A N   
112  C CA  . LEU A 16  ? 0.3635 0.2852 0.3927 0.0276  -0.0142 -0.0125 195 LEU A CA  
113  C C   . LEU A 16  ? 0.3754 0.2924 0.3995 0.0161  -0.0137 -0.0110 195 LEU A C   
114  O O   . LEU A 16  ? 0.3761 0.2824 0.3981 0.0118  -0.0154 -0.0026 195 LEU A O   
115  C CB  . LEU A 16  ? 0.3616 0.2674 0.3968 0.0350  -0.0149 -0.0201 195 LEU A CB  
116  C CG  . LEU A 16  ? 0.3586 0.2676 0.4015 0.0475  -0.0166 -0.0196 195 LEU A CG  
117  C CD1 . LEU A 16  ? 0.3618 0.2515 0.4122 0.0555  -0.0180 -0.0259 195 LEU A CD1 
118  C CD2 . LEU A 16  ? 0.3688 0.2790 0.4099 0.0491  -0.0205 -0.0057 195 LEU A CD2 
119  N N   . GLU A 17  ? 0.3755 0.3019 0.3975 0.0107  -0.0116 -0.0187 196 GLU A N   
120  C CA  . GLU A 17  ? 0.3900 0.3144 0.4089 -0.0001 -0.0118 -0.0184 196 GLU A CA  
121  C C   . GLU A 17  ? 0.3818 0.3221 0.3990 -0.0051 -0.0114 -0.0108 196 GLU A C   
122  O O   . GLU A 17  ? 0.3724 0.3131 0.3890 -0.0136 -0.0118 -0.0082 196 GLU A O   
123  C CB  . GLU A 17  ? 0.3999 0.3268 0.4170 -0.0043 -0.0107 -0.0303 196 GLU A CB  
124  C CG  . GLU A 17  ? 0.4273 0.3362 0.4463 -0.0012 -0.0103 -0.0397 196 GLU A CG  
125  C CD  . GLU A 17  ? 0.4462 0.3570 0.4616 -0.0069 -0.0090 -0.0525 196 GLU A CD  
126  O OE1 . GLU A 17  ? 0.4555 0.3816 0.4666 -0.0143 -0.0093 -0.0526 196 GLU A OE1 
127  O OE2 . GLU A 17  ? 0.4513 0.3486 0.4683 -0.0039 -0.0078 -0.0625 196 GLU A OE2 
128  N N   . TYR A 18  ? 0.3679 0.3217 0.3852 0.0001  -0.0106 -0.0077 197 TYR A N   
129  C CA  . TYR A 18  ? 0.3600 0.3285 0.3765 -0.0038 -0.0099 -0.0024 197 TYR A CA  
130  C C   . TYR A 18  ? 0.3514 0.3254 0.3677 0.0009  -0.0094 0.0047  197 TYR A C   
131  O O   . TYR A 18  ? 0.3460 0.3209 0.3617 -0.0026 -0.0090 0.0116  197 TYR A O   
132  C CB  . TYR A 18  ? 0.3750 0.3572 0.3902 -0.0059 -0.0095 -0.0078 197 TYR A CB  
133  C CG  . TYR A 18  ? 0.3921 0.3871 0.4081 -0.0099 -0.0095 -0.0026 197 TYR A CG  
134  C CD1 . TYR A 18  ? 0.3944 0.3897 0.4127 -0.0170 -0.0102 -0.0001 197 TYR A CD1 
135  C CD2 . TYR A 18  ? 0.3878 0.3943 0.4034 -0.0066 -0.0086 -0.0005 197 TYR A CD2 
136  C CE1 . TYR A 18  ? 0.4022 0.4105 0.4237 -0.0195 -0.0101 0.0041  197 TYR A CE1 
137  C CE2 . TYR A 18  ? 0.3989 0.4156 0.4166 -0.0091 -0.0086 0.0038  197 TYR A CE2 
138  C CZ  . TYR A 18  ? 0.4181 0.4362 0.4394 -0.0149 -0.0094 0.0060  197 TYR A CZ  
139  O OH  . TYR A 18  ? 0.4570 0.4865 0.4828 -0.0163 -0.0093 0.0095  197 TYR A OH  
140  N N   . ILE A 19  ? 0.3313 0.3107 0.3482 0.0078  -0.0091 0.0024  198 ILE A N   
141  C CA  . ILE A 19  ? 0.3296 0.3170 0.3459 0.0111  -0.0087 0.0079  198 ILE A CA  
142  C C   . ILE A 19  ? 0.3327 0.3105 0.3477 0.0120  -0.0103 0.0155  198 ILE A C   
143  O O   . ILE A 19  ? 0.3296 0.3120 0.3421 0.0091  -0.0095 0.0215  198 ILE A O   
144  C CB  . ILE A 19  ? 0.3135 0.3094 0.3312 0.0173  -0.0082 0.0035  198 ILE A CB  
145  C CG1 . ILE A 19  ? 0.3169 0.3228 0.3334 0.0147  -0.0064 -0.0023 198 ILE A CG1 
146  C CG2 . ILE A 19  ? 0.2994 0.3026 0.3164 0.0200  -0.0083 0.0088  198 ILE A CG2 
147  C CD1 . ILE A 19  ? 0.3201 0.3349 0.3378 0.0191  -0.0050 -0.0072 198 ILE A CD1 
148  N N   . VAL A 20  ? 0.3396 0.3039 0.3562 0.0160  -0.0126 0.0151  199 VAL A N   
149  C CA  . VAL A 20  ? 0.3501 0.3037 0.3646 0.0175  -0.0152 0.0235  199 VAL A CA  
150  C C   . VAL A 20  ? 0.3637 0.3122 0.3738 0.0084  -0.0142 0.0300  199 VAL A C   
151  O O   . VAL A 20  ? 0.3654 0.3182 0.3712 0.0063  -0.0139 0.0373  199 VAL A O   
152  C CB  . VAL A 20  ? 0.3520 0.2900 0.3703 0.0244  -0.0185 0.0220  199 VAL A CB  
153  C CG1 . VAL A 20  ? 0.3651 0.2873 0.3799 0.0237  -0.0220 0.0323  199 VAL A CG1 
154  C CG2 . VAL A 20  ? 0.3466 0.2937 0.3704 0.0341  -0.0195 0.0176  199 VAL A CG2 
155  N N   . PRO A 21  ? 0.3800 0.3206 0.3910 0.0020  -0.0134 0.0273  200 PRO A N   
156  C CA  . PRO A 21  ? 0.3910 0.3293 0.3991 -0.0076 -0.0120 0.0330  200 PRO A CA  
157  C C   . PRO A 21  ? 0.3873 0.3444 0.3952 -0.0113 -0.0087 0.0345  200 PRO A C   
158  O O   . PRO A 21  ? 0.3751 0.3344 0.3794 -0.0159 -0.0071 0.0412  200 PRO A O   
159  C CB  . PRO A 21  ? 0.3927 0.3229 0.4034 -0.0137 -0.0119 0.0272  200 PRO A CB  
160  C CG  . PRO A 21  ? 0.3926 0.3258 0.4066 -0.0076 -0.0124 0.0172  200 PRO A CG  
161  C CD  . PRO A 21  ? 0.3865 0.3208 0.4010 0.0028  -0.0137 0.0180  200 PRO A CD  
162  N N   . CYS A 22  ? 0.3874 0.3575 0.3987 -0.0091 -0.0076 0.0281  201 CYS A N   
163  C CA  . CYS A 22  ? 0.3888 0.3751 0.4015 -0.0113 -0.0049 0.0286  201 CYS A CA  
164  C C   . CYS A 22  ? 0.3786 0.3703 0.3875 -0.0084 -0.0037 0.0334  201 CYS A C   
165  O O   . CYS A 22  ? 0.3747 0.3742 0.3830 -0.0125 -0.0007 0.0363  201 CYS A O   
166  C CB  . CYS A 22  ? 0.4380 0.4341 0.4539 -0.0086 -0.0051 0.0220  201 CYS A CB  
167  S SG  . CYS A 22  ? 0.5357 0.5478 0.5564 -0.0128 -0.0030 0.0218  201 CYS A SG  
168  N N   . MET A 23  ? 0.3718 0.3602 0.3785 -0.0017 -0.0059 0.0335  202 MET A N   
169  C CA  . MET A 23  ? 0.3661 0.3606 0.3687 0.0008  -0.0056 0.0372  202 MET A CA  
170  C C   . MET A 23  ? 0.3700 0.3576 0.3662 -0.0030 -0.0060 0.0455  202 MET A C   
171  O O   . MET A 23  ? 0.3593 0.3547 0.3510 -0.0061 -0.0035 0.0485  202 MET A O   
172  C CB  . MET A 23  ? 0.3550 0.3500 0.3585 0.0087  -0.0085 0.0349  202 MET A CB  
173  C CG  . MET A 23  ? 0.3368 0.3424 0.3440 0.0112  -0.0071 0.0280  202 MET A CG  
174  S SD  . MET A 23  ? 0.3201 0.3394 0.3257 0.0086  -0.0035 0.0278  202 MET A SD  
175  C CE  . MET A 23  ? 0.3145 0.3368 0.3149 0.0113  -0.0052 0.0316  202 MET A CE  
176  N N   . ASN A 24  ? 0.3839 0.3561 0.3790 -0.0035 -0.0089 0.0490  203 ASN A N   
177  C CA  . ASN A 24  ? 0.4013 0.3646 0.3889 -0.0077 -0.0101 0.0584  203 ASN A CA  
178  C C   . ASN A 24  ? 0.4054 0.3732 0.3909 -0.0179 -0.0052 0.0608  203 ASN A C   
179  O O   . ASN A 24  ? 0.4132 0.3807 0.3908 -0.0230 -0.0041 0.0681  203 ASN A O   
180  C CB  . ASN A 24  ? 0.4106 0.3537 0.3979 -0.0051 -0.0149 0.0621  203 ASN A CB  
181  C CG  . ASN A 24  ? 0.4171 0.3579 0.4067 0.0057  -0.0198 0.0616  203 ASN A CG  
182  O OD1 . ASN A 24  ? 0.4099 0.3606 0.3963 0.0089  -0.0211 0.0642  203 ASN A OD1 
183  N ND2 . ASN A 24  ? 0.4194 0.3480 0.4151 0.0111  -0.0225 0.0574  203 ASN A ND2 
184  N N   . LYS A 25  ? 0.3962 0.3695 0.3889 -0.0212 -0.0025 0.0547  204 LYS A N   
185  C CA  . LYS A 25  ? 0.4023 0.3821 0.3962 -0.0306 0.0020  0.0559  204 LYS A CA  
186  C C   . LYS A 25  ? 0.3781 0.3773 0.3745 -0.0306 0.0066  0.0528  204 LYS A C   
187  O O   . LYS A 25  ? 0.3525 0.3590 0.3463 -0.0368 0.0110  0.0558  204 LYS A O   
188  C CB  . LYS A 25  ? 0.4360 0.4122 0.4372 -0.0349 0.0016  0.0515  204 LYS A CB  
189  C CG  . LYS A 25  ? 0.4989 0.4544 0.4974 -0.0384 -0.0014 0.0547  204 LYS A CG  
190  C CD  . LYS A 25  ? 0.5272 0.4800 0.5320 -0.0446 -0.0015 0.0495  204 LYS A CD  
191  C CE  . LYS A 25  ? 0.5473 0.5023 0.5575 -0.0384 -0.0038 0.0403  204 LYS A CE  
192  N NZ  . LYS A 25  ? 0.5688 0.5212 0.5837 -0.0455 -0.0045 0.0351  204 LYS A NZ  
193  N N   . HIS A 26  ? 0.3578 0.3647 0.3592 -0.0239 0.0060  0.0465  205 HIS A N   
194  C CA  . HIS A 26  ? 0.3532 0.3760 0.3594 -0.0235 0.0100  0.0424  205 HIS A CA  
195  C C   . HIS A 26  ? 0.3341 0.3616 0.3366 -0.0175 0.0101  0.0410  205 HIS A C   
196  O O   . HIS A 26  ? 0.3251 0.3634 0.3293 -0.0175 0.0139  0.0383  205 HIS A O   
197  C CB  . HIS A 26  ? 0.3763 0.4047 0.3924 -0.0225 0.0092  0.0368  205 HIS A CB  
198  C CG  . HIS A 26  ? 0.4221 0.4477 0.4425 -0.0292 0.0087  0.0372  205 HIS A CG  
199  N ND1 . HIS A 26  ? 0.4438 0.4734 0.4654 -0.0372 0.0123  0.0404  205 HIS A ND1 
200  C CD2 . HIS A 26  ? 0.4375 0.4571 0.4610 -0.0300 0.0053  0.0344  205 HIS A CD2 
201  C CE1 . HIS A 26  ? 0.4608 0.4868 0.4867 -0.0429 0.0107  0.0396  205 HIS A CE1 
202  N NE2 . HIS A 26  ? 0.4556 0.4752 0.4823 -0.0385 0.0063  0.0357  205 HIS A NE2 
203  N N   . GLY A 27  ? 0.3294 0.3491 0.3276 -0.0125 0.0059  0.0420  206 GLY A N   
204  C CA  . GLY A 27  ? 0.3286 0.3533 0.3235 -0.0077 0.0053  0.0405  206 GLY A CA  
205  C C   . GLY A 27  ? 0.3211 0.3526 0.3221 -0.0039 0.0059  0.0340  206 GLY A C   
206  O O   . GLY A 27  ? 0.3152 0.3516 0.3143 -0.0011 0.0062  0.0319  206 GLY A O   
207  N N   . ILE A 28  ? 0.3001 0.3317 0.3078 -0.0045 0.0058  0.0313  207 ILE A N   
208  C CA  . ILE A 28  ? 0.3086 0.3456 0.3215 -0.0019 0.0057  0.0267  207 ILE A CA  
209  C C   . ILE A 28  ? 0.3066 0.3389 0.3226 -0.0020 0.0027  0.0249  207 ILE A C   
210  O O   . ILE A 28  ? 0.3068 0.3352 0.3242 -0.0059 0.0023  0.0263  207 ILE A O   
211  C CB  . ILE A 28  ? 0.3078 0.3536 0.3261 -0.0036 0.0092  0.0254  207 ILE A CB  
212  C CG1 . ILE A 28  ? 0.3118 0.3624 0.3266 -0.0040 0.0131  0.0254  207 ILE A CG1 
213  C CG2 . ILE A 28  ? 0.3069 0.3563 0.3304 -0.0009 0.0079  0.0223  207 ILE A CG2 
214  C CD1 . ILE A 28  ? 0.3213 0.3805 0.3427 -0.0056 0.0176  0.0236  207 ILE A CD1 
215  N N   . CYS A 29  ? 0.3033 0.3365 0.3196 0.0012  0.0010  0.0215  208 CYS A N   
216  C CA  . CYS A 29  ? 0.3098 0.3397 0.3274 0.0007  -0.0014 0.0185  208 CYS A CA  
217  C C   . CYS A 29  ? 0.2995 0.3354 0.3176 0.0020  -0.0021 0.0156  208 CYS A C   
218  O O   . CYS A 29  ? 0.3004 0.3383 0.3162 0.0048  -0.0016 0.0145  208 CYS A O   
219  C CB  . CYS A 29  ? 0.3105 0.3318 0.3255 0.0032  -0.0031 0.0173  208 CYS A CB  
220  S SG  . CYS A 29  ? 0.3331 0.3501 0.3488 0.0022  -0.0051 0.0114  208 CYS A SG  
221  N N   . VAL A 30  ? 0.2953 0.3343 0.3162 -0.0008 -0.0035 0.0148  209 VAL A N   
222  C CA  . VAL A 30  ? 0.3057 0.3497 0.3260 -0.0005 -0.0050 0.0136  209 VAL A CA  
223  C C   . VAL A 30  ? 0.3094 0.3512 0.3261 -0.0023 -0.0071 0.0096  209 VAL A C   
224  O O   . VAL A 30  ? 0.2891 0.3283 0.3071 -0.0055 -0.0085 0.0082  209 VAL A O   
225  C CB  . VAL A 30  ? 0.3240 0.3746 0.3501 -0.0018 -0.0061 0.0161  209 VAL A CB  
226  C CG1 . VAL A 30  ? 0.3233 0.3777 0.3477 -0.0019 -0.0090 0.0164  209 VAL A CG1 
227  C CG2 . VAL A 30  ? 0.3288 0.3819 0.3588 0.0002  -0.0030 0.0183  209 VAL A CG2 
228  N N   . VAL A 31  ? 0.3138 0.3573 0.3259 -0.0011 -0.0070 0.0072  210 VAL A N   
229  C CA  . VAL A 31  ? 0.3221 0.3654 0.3297 -0.0031 -0.0080 0.0022  210 VAL A CA  
230  C C   . VAL A 31  ? 0.3305 0.3803 0.3336 -0.0053 -0.0094 0.0032  210 VAL A C   
231  O O   . VAL A 31  ? 0.3325 0.3846 0.3331 -0.0039 -0.0078 0.0042  210 VAL A O   
232  C CB  . VAL A 31  ? 0.3297 0.3694 0.3358 0.0002  -0.0058 -0.0026 210 VAL A CB  
233  C CG1 . VAL A 31  ? 0.3448 0.3855 0.3465 -0.0017 -0.0056 -0.0095 210 VAL A CG1 
234  C CG2 . VAL A 31  ? 0.3220 0.3534 0.3319 0.0027  -0.0055 -0.0020 210 VAL A CG2 
235  N N   . ASP A 32  ? 0.3255 0.3784 0.3273 -0.0093 -0.0128 0.0034  211 ASP A N   
236  C CA  . ASP A 32  ? 0.3319 0.3904 0.3279 -0.0120 -0.0153 0.0056  211 ASP A CA  
237  C C   . ASP A 32  ? 0.3343 0.3944 0.3211 -0.0151 -0.0143 -0.0006 211 ASP A C   
238  O O   . ASP A 32  ? 0.3182 0.3750 0.3049 -0.0153 -0.0126 -0.0073 211 ASP A O   
239  C CB  . ASP A 32  ? 0.3522 0.4155 0.3516 -0.0143 -0.0204 0.0100  211 ASP A CB  
240  C CG  . ASP A 32  ? 0.3734 0.4376 0.3813 -0.0106 -0.0209 0.0162  211 ASP A CG  
241  O OD1 . ASP A 32  ? 0.3789 0.4415 0.3851 -0.0082 -0.0196 0.0192  211 ASP A OD1 
242  O OD2 . ASP A 32  ? 0.3869 0.4538 0.4033 -0.0104 -0.0222 0.0175  211 ASP A OD2 
243  N N   . ASP A 33  ? 0.3389 0.4036 0.3180 -0.0178 -0.0151 0.0017  212 ASP A N   
244  C CA  . ASP A 33  ? 0.3640 0.4330 0.3326 -0.0223 -0.0138 -0.0037 212 ASP A CA  
245  C C   . ASP A 33  ? 0.3636 0.4315 0.3330 -0.0195 -0.0079 -0.0115 212 ASP A C   
246  O O   . ASP A 33  ? 0.3642 0.4331 0.3301 -0.0212 -0.0061 -0.0199 212 ASP A O   
247  C CB  . ASP A 33  ? 0.3967 0.4683 0.3606 -0.0275 -0.0176 -0.0070 212 ASP A CB  
248  C CG  . ASP A 33  ? 0.4181 0.4933 0.3828 -0.0297 -0.0244 0.0012  212 ASP A CG  
249  O OD1 . ASP A 33  ? 0.4440 0.5213 0.4053 -0.0300 -0.0265 0.0086  212 ASP A OD1 
250  O OD2 . ASP A 33  ? 0.4540 0.5299 0.4234 -0.0312 -0.0278 0.0001  212 ASP A OD2 
251  N N   . PHE A 34  ? 0.3516 0.4183 0.3262 -0.0152 -0.0052 -0.0092 213 PHE A N   
252  C CA  . PHE A 34  ? 0.3480 0.4147 0.3267 -0.0111 -0.0007 -0.0156 213 PHE A CA  
253  C C   . PHE A 34  ? 0.3520 0.4267 0.3239 -0.0141 0.0032  -0.0222 213 PHE A C   
254  O O   . PHE A 34  ? 0.3540 0.4294 0.3277 -0.0121 0.0060  -0.0310 213 PHE A O   
255  C CB  . PHE A 34  ? 0.3290 0.3942 0.3144 -0.0065 0.0004  -0.0114 213 PHE A CB  
256  C CG  . PHE A 34  ? 0.3102 0.3771 0.3009 -0.0017 0.0037  -0.0168 213 PHE A CG  
257  C CD1 . PHE A 34  ? 0.3064 0.3694 0.3010 0.0018  0.0043  -0.0231 213 PHE A CD1 
258  C CD2 . PHE A 34  ? 0.3008 0.3731 0.2935 -0.0007 0.0059  -0.0155 213 PHE A CD2 
259  C CE1 . PHE A 34  ? 0.3019 0.3669 0.3031 0.0075  0.0065  -0.0275 213 PHE A CE1 
260  C CE2 . PHE A 34  ? 0.2929 0.3692 0.2920 0.0042  0.0080  -0.0202 213 PHE A CE2 
261  C CZ  . PHE A 34  ? 0.2922 0.3650 0.2961 0.0089  0.0081  -0.0259 213 PHE A CZ  
262  N N   . LEU A 35  ? 0.3380 0.4185 0.3024 -0.0191 0.0035  -0.0180 214 LEU A N   
263  C CA  . LEU A 35  ? 0.3531 0.4431 0.3114 -0.0228 0.0084  -0.0235 214 LEU A CA  
264  C C   . LEU A 35  ? 0.3563 0.4508 0.3008 -0.0311 0.0073  -0.0235 214 LEU A C   
265  O O   . LEU A 35  ? 0.3530 0.4561 0.2908 -0.0351 0.0119  -0.0305 214 LEU A O   
266  C CB  . LEU A 35  ? 0.3416 0.4351 0.3012 -0.0235 0.0106  -0.0189 214 LEU A CB  
267  C CG  . LEU A 35  ? 0.3307 0.4236 0.3024 -0.0165 0.0123  -0.0204 214 LEU A CG  
268  C CD1 . LEU A 35  ? 0.3161 0.4147 0.2875 -0.0193 0.0149  -0.0175 214 LEU A CD1 
269  C CD2 . LEU A 35  ? 0.3372 0.4339 0.3156 -0.0113 0.0154  -0.0305 214 LEU A CD2 
270  N N   . GLY A 36  ? 0.3692 0.4592 0.3095 -0.0336 0.0011  -0.0155 215 GLY A N   
271  C CA  . GLY A 36  ? 0.3771 0.4716 0.3034 -0.0417 -0.0017 -0.0132 215 GLY A CA  
272  C C   . GLY A 36  ? 0.3946 0.4899 0.3131 -0.0464 -0.0032 -0.0029 215 GLY A C   
273  O O   . GLY A 36  ? 0.3967 0.4904 0.3200 -0.0445 -0.0003 -0.0001 215 GLY A O   
274  N N   . LYS A 37  ? 0.4105 0.5079 0.3165 -0.0532 -0.0081 0.0028  216 LYS A N   
275  C CA  . LYS A 37  ? 0.4389 0.5335 0.3373 -0.0573 -0.0120 0.0152  216 LYS A CA  
276  C C   . LYS A 37  ? 0.4443 0.5428 0.3351 -0.0629 -0.0056 0.0150  216 LYS A C   
277  O O   . LYS A 37  ? 0.4467 0.5391 0.3391 -0.0630 -0.0060 0.0231  216 LYS A O   
278  C CB  . LYS A 37  ? 0.4711 0.5681 0.3571 -0.0633 -0.0195 0.0213  216 LYS A CB  
279  C CG  . LYS A 37  ? 0.5090 0.6013 0.3867 -0.0672 -0.0253 0.0358  216 LYS A CG  
280  C CD  . LYS A 37  ? 0.5330 0.6262 0.4054 -0.0690 -0.0357 0.0440  216 LYS A CD  
281  C CE  . LYS A 37  ? 0.5733 0.6774 0.4302 -0.0774 -0.0369 0.0385  216 LYS A CE  
282  N NZ  . LYS A 37  ? 0.5961 0.7023 0.4483 -0.0793 -0.0483 0.0475  216 LYS A NZ  
283  N N   . GLU A 38  ? 0.4425 0.5518 0.3257 -0.0680 0.0007  0.0052  217 GLU A N   
284  C CA  . GLU A 38  ? 0.4399 0.5564 0.3150 -0.0751 0.0073  0.0046  217 GLU A CA  
285  C C   . GLU A 38  ? 0.4197 0.5348 0.3089 -0.0697 0.0122  0.0025  217 GLU A C   
286  O O   . GLU A 38  ? 0.4155 0.5279 0.3024 -0.0736 0.0130  0.0097  217 GLU A O   
287  C CB  . GLU A 38  ? 0.4751 0.6056 0.3404 -0.0813 0.0140  -0.0072 217 GLU A CB  
288  C CG  . GLU A 38  ? 0.5062 0.6471 0.3658 -0.0886 0.0223  -0.0094 217 GLU A CG  
289  C CD  . GLU A 38  ? 0.5355 0.6925 0.3845 -0.0958 0.0300  -0.0214 217 GLU A CD  
290  O OE1 . GLU A 38  ? 0.5506 0.7144 0.3829 -0.1075 0.0325  -0.0170 217 GLU A OE1 
291  O OE2 . GLU A 38  ? 0.5507 0.7128 0.4080 -0.0900 0.0339  -0.0351 217 GLU A OE2 
292  N N   . THR A 39  ? 0.4013 0.5180 0.3045 -0.0611 0.0150  -0.0072 218 THR A N   
293  C CA  . THR A 39  ? 0.3898 0.5070 0.3066 -0.0555 0.0187  -0.0099 218 THR A CA  
294  C C   . THR A 39  ? 0.3803 0.4850 0.3024 -0.0525 0.0137  0.0008  218 THR A C   
295  O O   . THR A 39  ? 0.3813 0.4857 0.3066 -0.0538 0.0161  0.0032  218 THR A O   
296  C CB  . THR A 39  ? 0.3923 0.5120 0.3222 -0.0465 0.0211  -0.0208 218 THR A CB  
297  O OG1 . THR A 39  ? 0.3818 0.5126 0.3067 -0.0494 0.0263  -0.0316 218 THR A OG1 
298  C CG2 . THR A 39  ? 0.3782 0.5004 0.3217 -0.0406 0.0241  -0.0233 218 THR A CG2 
299  N N   . GLY A 40  ? 0.3866 0.4818 0.3099 -0.0488 0.0071  0.0062  219 GLY A N   
300  C CA  . GLY A 40  ? 0.4000 0.4837 0.3295 -0.0449 0.0025  0.0150  219 GLY A CA  
301  C C   . GLY A 40  ? 0.4095 0.4879 0.3305 -0.0514 0.0013  0.0247  219 GLY A C   
302  O O   . GLY A 40  ? 0.3873 0.4584 0.3139 -0.0497 0.0015  0.0284  219 GLY A O   
303  N N   . GLN A 41  ? 0.4174 0.4988 0.3239 -0.0595 -0.0001 0.0287  220 GLN A N   
304  C CA  . GLN A 41  ? 0.4412 0.5161 0.3373 -0.0669 -0.0020 0.0393  220 GLN A CA  
305  C C   . GLN A 41  ? 0.4253 0.5044 0.3204 -0.0726 0.0053  0.0365  220 GLN A C   
306  O O   . GLN A 41  ? 0.4214 0.4908 0.3161 -0.0753 0.0047  0.0435  220 GLN A O   
307  C CB  . GLN A 41  ? 0.5008 0.5792 0.3798 -0.0749 -0.0057 0.0445  220 GLN A CB  
308  C CG  . GLN A 41  ? 0.5732 0.6415 0.4407 -0.0819 -0.0099 0.0585  220 GLN A CG  
309  C CD  . GLN A 41  ? 0.6313 0.6846 0.5067 -0.0746 -0.0183 0.0685  220 GLN A CD  
310  O OE1 . GLN A 41  ? 0.6705 0.7234 0.5576 -0.0656 -0.0218 0.0659  220 GLN A OE1 
311  N NE2 . GLN A 41  ? 0.6617 0.7025 0.5310 -0.0786 -0.0214 0.0801  220 GLN A NE2 
312  N N   . GLN A 42  ? 0.4027 0.4968 0.2985 -0.0744 0.0122  0.0255  221 GLN A N   
313  C CA  . GLN A 42  ? 0.4068 0.5097 0.3039 -0.0798 0.0196  0.0211  221 GLN A CA  
314  C C   . GLN A 42  ? 0.3845 0.4816 0.2962 -0.0735 0.0199  0.0202  221 GLN A C   
315  O O   . GLN A 42  ? 0.3652 0.4613 0.2765 -0.0792 0.0226  0.0225  221 GLN A O   
316  C CB  . GLN A 42  ? 0.4453 0.5667 0.3437 -0.0805 0.0266  0.0082  221 GLN A CB  
317  C CG  . GLN A 42  ? 0.5135 0.6427 0.3952 -0.0891 0.0279  0.0076  221 GLN A CG  
318  C CD  . GLN A 42  ? 0.5474 0.6959 0.4307 -0.0907 0.0366  -0.0064 221 GLN A CD  
319  O OE1 . GLN A 42  ? 0.5691 0.7222 0.4539 -0.0861 0.0371  -0.0151 221 GLN A OE1 
320  N NE2 . GLN A 42  ? 0.5750 0.7351 0.4589 -0.0973 0.0437  -0.0092 221 GLN A NE2 
321  N N   . ILE A 43  ? 0.3701 0.4637 0.2936 -0.0626 0.0171  0.0167  222 ILE A N   
322  C CA  . ILE A 43  ? 0.3558 0.4435 0.2915 -0.0565 0.0166  0.0162  222 ILE A CA  
323  C C   . ILE A 43  ? 0.3624 0.4345 0.2947 -0.0592 0.0130  0.0262  222 ILE A C   
324  O O   . ILE A 43  ? 0.3731 0.4422 0.3082 -0.0620 0.0151  0.0266  222 ILE A O   
325  C CB  . ILE A 43  ? 0.3684 0.4536 0.3144 -0.0456 0.0137  0.0125  222 ILE A CB  
326  C CG1 . ILE A 43  ? 0.3722 0.4697 0.3226 -0.0420 0.0169  0.0025  222 ILE A CG1 
327  C CG2 . ILE A 43  ? 0.3495 0.4280 0.3054 -0.0403 0.0129  0.0132  222 ILE A CG2 
328  C CD1 . ILE A 43  ? 0.3920 0.4995 0.3521 -0.0395 0.0212  -0.0045 222 ILE A CD1 
329  N N   . GLY A 44  ? 0.3614 0.4235 0.2881 -0.0583 0.0073  0.0340  223 GLY A N   
330  C CA  . GLY A 44  ? 0.3615 0.4074 0.2859 -0.0593 0.0029  0.0440  223 GLY A CA  
331  C C   . GLY A 44  ? 0.3702 0.4124 0.2851 -0.0702 0.0056  0.0487  223 GLY A C   
332  O O   . GLY A 44  ? 0.3709 0.4007 0.2884 -0.0711 0.0052  0.0524  223 GLY A O   
333  N N   . ASP A 45  ? 0.3777 0.4310 0.2814 -0.0791 0.0089  0.0480  224 ASP A N   
334  C CA  . ASP A 45  ? 0.3803 0.4328 0.2735 -0.0915 0.0123  0.0524  224 ASP A CA  
335  C C   . ASP A 45  ? 0.3646 0.4215 0.2668 -0.0935 0.0181  0.0456  224 ASP A C   
336  O O   . ASP A 45  ? 0.3726 0.4185 0.2724 -0.0998 0.0185  0.0507  224 ASP A O   
337  C CB  . ASP A 45  ? 0.3978 0.4647 0.2774 -0.1006 0.0157  0.0512  224 ASP A CB  
338  C CG  . ASP A 45  ? 0.4258 0.4874 0.2928 -0.1018 0.0091  0.0599  224 ASP A CG  
339  O OD1 . ASP A 45  ? 0.4364 0.4814 0.3045 -0.0970 0.0016  0.0693  224 ASP A OD1 
340  O OD2 . ASP A 45  ? 0.4413 0.5162 0.2979 -0.1073 0.0115  0.0566  224 ASP A OD2 
341  N N   . GLU A 46  ? 0.3448 0.4177 0.2576 -0.0880 0.0220  0.0343  225 GLU A N   
342  C CA  . GLU A 46  ? 0.3369 0.4185 0.2591 -0.0896 0.0268  0.0273  225 GLU A CA  
343  C C   . GLU A 46  ? 0.3367 0.4028 0.2663 -0.0850 0.0237  0.0294  225 GLU A C   
344  O O   . GLU A 46  ? 0.3381 0.4027 0.2692 -0.0913 0.0262  0.0286  225 GLU A O   
345  C CB  . GLU A 46  ? 0.3361 0.4369 0.2689 -0.0826 0.0301  0.0158  225 GLU A CB  
346  C CG  . GLU A 46  ? 0.3523 0.4703 0.2792 -0.0876 0.0348  0.0109  225 GLU A CG  
347  C CD  . GLU A 46  ? 0.3486 0.4850 0.2876 -0.0801 0.0384  -0.0011 225 GLU A CD  
348  O OE1 . GLU A 46  ? 0.3475 0.4828 0.2989 -0.0708 0.0362  -0.0045 225 GLU A OE1 
349  O OE2 . GLU A 46  ? 0.3525 0.5040 0.2883 -0.0837 0.0433  -0.0070 225 GLU A OE2 
350  N N   . VAL A 47  ? 0.3284 0.3840 0.2626 -0.0747 0.0187  0.0314  226 VAL A N   
351  C CA  . VAL A 47  ? 0.3390 0.3815 0.2807 -0.0693 0.0165  0.0318  226 VAL A CA  
352  C C   . VAL A 47  ? 0.3510 0.3741 0.2859 -0.0756 0.0146  0.0404  226 VAL A C   
353  O O   . VAL A 47  ? 0.3496 0.3644 0.2880 -0.0776 0.0158  0.0389  226 VAL A O   
354  C CB  . VAL A 47  ? 0.3374 0.3763 0.2863 -0.0573 0.0125  0.0312  226 VAL A CB  
355  C CG1 . VAL A 47  ? 0.3389 0.3636 0.2942 -0.0524 0.0107  0.0319  226 VAL A CG1 
356  C CG2 . VAL A 47  ? 0.3207 0.3755 0.2768 -0.0513 0.0143  0.0228  226 VAL A CG2 
357  N N   . ARG A 48  ? 0.3638 0.3792 0.2886 -0.0788 0.0114  0.0495  227 ARG A N   
358  C CA  . ARG A 48  ? 0.3898 0.3849 0.3074 -0.0846 0.0086  0.0594  227 ARG A CA  
359  C C   . ARG A 48  ? 0.3878 0.3835 0.2994 -0.0979 0.0137  0.0590  227 ARG A C   
360  O O   . ARG A 48  ? 0.3933 0.3715 0.3044 -0.1018 0.0133  0.0624  227 ARG A O   
361  C CB  . ARG A 48  ? 0.4167 0.4054 0.3239 -0.0853 0.0031  0.0702  227 ARG A CB  
362  C CG  . ARG A 48  ? 0.4470 0.4280 0.3617 -0.0729 -0.0035 0.0732  227 ARG A CG  
363  C CD  . ARG A 48  ? 0.4754 0.4516 0.3808 -0.0733 -0.0104 0.0842  227 ARG A CD  
364  N NE  . ARG A 48  ? 0.4898 0.4841 0.3864 -0.0775 -0.0092 0.0820  227 ARG A NE  
365  C CZ  . ARG A 48  ? 0.4953 0.5006 0.3962 -0.0705 -0.0114 0.0777  227 ARG A CZ  
366  N NH1 . ARG A 48  ? 0.4956 0.4975 0.4100 -0.0592 -0.0144 0.0754  227 ARG A NH1 
367  N NH2 . ARG A 48  ? 0.4911 0.5112 0.3827 -0.0755 -0.0099 0.0751  227 ARG A NH2 
368  N N   . ALA A 49  ? 0.3817 0.3981 0.2898 -0.1049 0.0189  0.0540  228 ALA A N   
369  C CA  . ALA A 49  ? 0.3770 0.3995 0.2809 -0.1185 0.0246  0.0524  228 ALA A CA  
370  C C   . ALA A 49  ? 0.3691 0.3912 0.2843 -0.1176 0.0268  0.0447  228 ALA A C   
371  O O   . ALA A 49  ? 0.3721 0.3832 0.2843 -0.1272 0.0283  0.0469  228 ALA A O   
372  C CB  . ALA A 49  ? 0.3768 0.4252 0.2782 -0.1238 0.0302  0.0464  228 ALA A CB  
373  N N   . LEU A 50  ? 0.3532 0.3868 0.2805 -0.1067 0.0267  0.0358  229 LEU A N   
374  C CA  . LEU A 50  ? 0.3433 0.3782 0.2805 -0.1050 0.0279  0.0284  229 LEU A CA  
375  C C   . LEU A 50  ? 0.3561 0.3646 0.2923 -0.1044 0.0249  0.0328  229 LEU A C   
376  O O   . LEU A 50  ? 0.3475 0.3506 0.2849 -0.1114 0.0269  0.0298  229 LEU A O   
377  C CB  . LEU A 50  ? 0.3316 0.3797 0.2796 -0.0922 0.0268  0.0209  229 LEU A CB  
378  C CG  . LEU A 50  ? 0.3208 0.3949 0.2733 -0.0915 0.0300  0.0143  229 LEU A CG  
379  C CD1 . LEU A 50  ? 0.3151 0.3965 0.2771 -0.0783 0.0277  0.0090  229 LEU A CD1 
380  C CD2 . LEU A 50  ? 0.3068 0.3967 0.2631 -0.1010 0.0344  0.0084  229 LEU A CD2 
381  N N   . HIS A 51  ? 0.3727 0.3656 0.3073 -0.0961 0.0202  0.0394  230 HIS A N   
382  C CA  . HIS A 51  ? 0.3981 0.3657 0.3336 -0.0933 0.0172  0.0434  230 HIS A CA  
383  C C   . HIS A 51  ? 0.4054 0.3559 0.3311 -0.1060 0.0177  0.0507  230 HIS A C   
384  O O   . HIS A 51  ? 0.4147 0.3500 0.3421 -0.1099 0.0187  0.0487  230 HIS A O   
385  C CB  . HIS A 51  ? 0.4206 0.3791 0.3584 -0.0814 0.0118  0.0490  230 HIS A CB  
386  C CG  . HIS A 51  ? 0.4611 0.3968 0.4039 -0.0753 0.0092  0.0508  230 HIS A CG  
387  N ND1 . HIS A 51  ? 0.4751 0.4015 0.4217 -0.0650 0.0041  0.0563  230 HIS A ND1 
388  C CD2 . HIS A 51  ? 0.4756 0.3969 0.4212 -0.0779 0.0110  0.0469  230 HIS A CD2 
389  C CE1 . HIS A 51  ? 0.4913 0.3986 0.4438 -0.0606 0.0033  0.0556  230 HIS A CE1 
390  N NE2 . HIS A 51  ? 0.4970 0.3998 0.4482 -0.0685 0.0076  0.0496  230 HIS A NE2 
391  N N   . ASP A 52  ? 0.4015 0.3544 0.3164 -0.1133 0.0172  0.0591  231 ASP A N   
392  C CA  . ASP A 52  ? 0.4196 0.3549 0.3228 -0.1259 0.0170  0.0687  231 ASP A CA  
393  C C   . ASP A 52  ? 0.4154 0.3561 0.3179 -0.1398 0.0231  0.0629  231 ASP A C   
394  O O   . ASP A 52  ? 0.4254 0.3450 0.3235 -0.1484 0.0231  0.0670  231 ASP A O   
395  C CB  . ASP A 52  ? 0.4247 0.3648 0.3147 -0.1314 0.0154  0.0787  231 ASP A CB  
396  C CG  . ASP A 52  ? 0.4454 0.3750 0.3339 -0.1204 0.0079  0.0874  231 ASP A CG  
397  O OD1 . ASP A 52  ? 0.4580 0.3732 0.3561 -0.1090 0.0039  0.0871  231 ASP A OD1 
398  O OD2 . ASP A 52  ? 0.4542 0.3918 0.3322 -0.1236 0.0061  0.0939  231 ASP A OD2 
399  N N   . THR A 53  ? 0.4008 0.3699 0.3084 -0.1419 0.0279  0.0532  232 THR A N   
400  C CA  . THR A 53  ? 0.3985 0.3789 0.3067 -0.1556 0.0335  0.0473  232 THR A CA  
401  C C   . THR A 53  ? 0.4007 0.3801 0.3200 -0.1522 0.0340  0.0371  232 THR A C   
402  O O   . THR A 53  ? 0.4015 0.3947 0.3243 -0.1617 0.0380  0.0301  232 THR A O   
403  C CB  . THR A 53  ? 0.3855 0.3980 0.2938 -0.1608 0.0385  0.0426  232 THR A CB  
404  O OG1 . THR A 53  ? 0.3846 0.4161 0.3042 -0.1470 0.0379  0.0341  232 THR A OG1 
405  C CG2 . THR A 53  ? 0.3888 0.4022 0.2835 -0.1670 0.0390  0.0521  232 THR A CG2 
406  N N   . GLY A 54  ? 0.4037 0.3688 0.3286 -0.1389 0.0300  0.0361  233 GLY A N   
407  C CA  . GLY A 54  ? 0.3946 0.3515 0.3268 -0.1363 0.0300  0.0280  233 GLY A CA  
408  C C   . GLY A 54  ? 0.3786 0.3622 0.3201 -0.1339 0.0321  0.0163  233 GLY A C   
409  O O   . GLY A 54  ? 0.3781 0.3634 0.3224 -0.1409 0.0339  0.0091  233 GLY A O   
410  N N   . LYS A 55  ? 0.3687 0.3721 0.3151 -0.1239 0.0313  0.0145  234 LYS A N   
411  C CA  . LYS A 55  ? 0.3571 0.3859 0.3125 -0.1204 0.0322  0.0051  234 LYS A CA  
412  C C   . LYS A 55  ? 0.3661 0.3904 0.3275 -0.1081 0.0295  0.0005  234 LYS A C   
413  O O   . LYS A 55  ? 0.3546 0.3972 0.3227 -0.1042 0.0292  -0.0063 234 LYS A O   
414  C CB  . LYS A 55  ? 0.3436 0.3961 0.3014 -0.1171 0.0333  0.0050  234 LYS A CB  
415  C CG  . LYS A 55  ? 0.3351 0.3980 0.2875 -0.1300 0.0374  0.0076  234 LYS A CG  
416  C CD  . LYS A 55  ? 0.3285 0.4029 0.2839 -0.1432 0.0408  0.0020  234 LYS A CD  
417  C CE  . LYS A 55  ? 0.3309 0.4130 0.2797 -0.1582 0.0456  0.0054  234 LYS A CE  
418  N NZ  . LYS A 55  ? 0.3219 0.4286 0.2732 -0.1549 0.0482  0.0037  234 LYS A NZ  
419  N N   . PHE A 56  ? 0.3661 0.3669 0.3252 -0.1020 0.0274  0.0045  235 PHE A N   
420  C CA  . PHE A 56  ? 0.3583 0.3553 0.3225 -0.0905 0.0256  0.0005  235 PHE A CA  
421  C C   . PHE A 56  ? 0.3572 0.3447 0.3221 -0.0948 0.0269  -0.0068 235 PHE A C   
422  O O   . PHE A 56  ? 0.3584 0.3298 0.3191 -0.1041 0.0282  -0.0063 235 PHE A O   
423  C CB  . PHE A 56  ? 0.3655 0.3455 0.3293 -0.0810 0.0230  0.0074  235 PHE A CB  
424  C CG  . PHE A 56  ? 0.3731 0.3643 0.3374 -0.0739 0.0211  0.0122  235 PHE A CG  
425  C CD1 . PHE A 56  ? 0.3780 0.3744 0.3366 -0.0797 0.0212  0.0179  235 PHE A CD1 
426  C CD2 . PHE A 56  ? 0.3785 0.3750 0.3484 -0.0624 0.0194  0.0105  235 PHE A CD2 
427  C CE1 . PHE A 56  ? 0.3775 0.3839 0.3359 -0.0737 0.0196  0.0210  235 PHE A CE1 
428  C CE2 . PHE A 56  ? 0.3839 0.3896 0.3542 -0.0568 0.0176  0.0142  235 PHE A CE2 
429  C CZ  . PHE A 56  ? 0.3788 0.3892 0.3434 -0.0623 0.0176  0.0190  235 PHE A CZ  
430  N N   . THR A 57  ? 0.3641 0.3611 0.3333 -0.0882 0.0264  -0.0136 236 THR A N   
431  C CA  . THR A 57  ? 0.3826 0.3723 0.3516 -0.0908 0.0276  -0.0218 236 THR A CA  
432  C C   . THR A 57  ? 0.4067 0.3828 0.3777 -0.0797 0.0274  -0.0225 236 THR A C   
433  O O   . THR A 57  ? 0.3840 0.3681 0.3582 -0.0697 0.0259  -0.0198 236 THR A O   
434  C CB  . THR A 57  ? 0.3778 0.3914 0.3490 -0.0930 0.0271  -0.0291 236 THR A CB  
435  O OG1 . THR A 57  ? 0.3842 0.4142 0.3563 -0.1019 0.0273  -0.0283 236 THR A OG1 
436  C CG2 . THR A 57  ? 0.3847 0.3930 0.3538 -0.0980 0.0282  -0.0384 236 THR A CG2 
437  N N   . ASP A 58  ? 0.4563 0.4125 0.4261 -0.0818 0.0292  -0.0271 237 ASP A N   
438  C CA  . ASP A 58  ? 0.5150 0.4578 0.4881 -0.0717 0.0300  -0.0292 237 ASP A CA  
439  C C   . ASP A 58  ? 0.5178 0.4780 0.4925 -0.0658 0.0305  -0.0352 237 ASP A C   
440  O O   . ASP A 58  ? 0.5049 0.4786 0.4767 -0.0717 0.0308  -0.0416 237 ASP A O   
441  C CB  . ASP A 58  ? 0.5770 0.4949 0.5490 -0.0758 0.0325  -0.0345 237 ASP A CB  
442  C CG  . ASP A 58  ? 0.6472 0.5446 0.6247 -0.0654 0.0324  -0.0310 237 ASP A CG  
443  O OD1 . ASP A 58  ? 0.6788 0.5697 0.6573 -0.0623 0.0293  -0.0203 237 ASP A OD1 
444  O OD2 . ASP A 58  ? 0.6889 0.5782 0.6696 -0.0605 0.0352  -0.0393 237 ASP A OD2 
445  N N   . GLY A 59  ? 0.5350 0.4950 0.5142 -0.0546 0.0301  -0.0325 238 GLY A N   
446  C CA  . GLY A 59  ? 0.5721 0.5483 0.5522 -0.0488 0.0303  -0.0356 238 GLY A CA  
447  C C   . GLY A 59  ? 0.6195 0.5946 0.5968 -0.0509 0.0337  -0.0464 238 GLY A C   
448  O O   . GLY A 59  ? 0.6206 0.6119 0.5943 -0.0520 0.0333  -0.0500 238 GLY A O   
449  N N   . GLN A 60  ? 0.6647 0.6200 0.6431 -0.0513 0.0369  -0.0517 239 GLN A N   
450  C CA  . GLN A 60  ? 0.7148 0.6677 0.6902 -0.0532 0.0411  -0.0635 239 GLN A CA  
451  C C   . GLN A 60  ? 0.7266 0.6835 0.6944 -0.0659 0.0410  -0.0703 239 GLN A C   
452  O O   . GLN A 60  ? 0.7324 0.6842 0.6960 -0.0705 0.0444  -0.0813 239 GLN A O   
453  C CB  . GLN A 60  ? 0.7534 0.6842 0.7346 -0.0475 0.0449  -0.0678 239 GLN A CB  
454  C CG  . GLN A 60  ? 0.7937 0.7240 0.7727 -0.0474 0.0505  -0.0812 239 GLN A CG  
455  C CD  . GLN A 60  ? 0.8050 0.7560 0.7826 -0.0428 0.0515  -0.0821 239 GLN A CD  
456  O OE1 . GLN A 60  ? 0.8172 0.7788 0.7984 -0.0367 0.0486  -0.0728 239 GLN A OE1 
457  N NE2 . GLN A 60  ? 0.8167 0.7727 0.7880 -0.0463 0.0559  -0.0935 239 GLN A NE2 
458  N N   . LEU A 61  ? 0.7038 0.6715 0.6703 -0.0717 0.0372  -0.0643 240 LEU A N   
459  C CA  . LEU A 61  ? 0.6705 0.6478 0.6316 -0.0838 0.0362  -0.0697 240 LEU A CA  
460  C C   . LEU A 61  ? 0.6569 0.6618 0.6168 -0.0830 0.0325  -0.0677 240 LEU A C   
461  O O   . LEU A 61  ? 0.6556 0.6737 0.6108 -0.0906 0.0312  -0.0738 240 LEU A O   
462  C CB  . LEU A 61  ? 0.6685 0.6373 0.6305 -0.0916 0.0352  -0.0646 240 LEU A CB  
463  C CG  . LEU A 61  ? 0.6698 0.6311 0.6274 -0.1057 0.0367  -0.0726 240 LEU A CG  
464  C CD1 . LEU A 61  ? 0.6583 0.6091 0.6165 -0.1133 0.0363  -0.0657 240 LEU A CD1 
465  C CD2 . LEU A 61  ? 0.6836 0.6697 0.6377 -0.1135 0.0347  -0.0789 240 LEU A CD2 
466  N N   . VAL A 62  ? 0.6506 0.6635 0.6146 -0.0736 0.0304  -0.0590 241 VAL A N   
467  C CA  . VAL A 62  ? 0.6727 0.7088 0.6368 -0.0711 0.0264  -0.0558 241 VAL A CA  
468  C C   . VAL A 62  ? 0.7096 0.7519 0.6693 -0.0669 0.0270  -0.0595 241 VAL A C   
469  O O   . VAL A 62  ? 0.7014 0.7617 0.6581 -0.0679 0.0235  -0.0594 241 VAL A O   
470  C CB  . VAL A 62  ? 0.6625 0.7039 0.6325 -0.0640 0.0240  -0.0458 241 VAL A CB  
471  C CG1 . VAL A 62  ? 0.6429 0.6745 0.6154 -0.0679 0.0247  -0.0416 241 VAL A CG1 
472  C CG2 . VAL A 62  ? 0.6825 0.7187 0.6547 -0.0533 0.0248  -0.0416 241 VAL A CG2 
473  N N   . SER A 63  ? 0.7523 0.7801 0.7120 -0.0623 0.0313  -0.0626 242 SER A N   
474  C CA  . SER A 63  ? 0.7934 0.8265 0.7487 -0.0587 0.0333  -0.0662 242 SER A CA  
475  C C   . SER A 63  ? 0.8131 0.8354 0.7634 -0.0637 0.0385  -0.0782 242 SER A C   
476  O O   . SER A 63  ? 0.8346 0.8674 0.7761 -0.0707 0.0380  -0.0849 242 SER A O   
477  C CB  . SER A 63  ? 0.8166 0.8463 0.7776 -0.0483 0.0345  -0.0598 242 SER A CB  
478  O OG  . SER A 63  ? 0.8367 0.8755 0.8016 -0.0443 0.0298  -0.0500 242 SER A OG  
479  N N   . ASP A 71  ? 0.9319 0.8707 0.9327 -0.0165 0.0751  -0.1130 250 ASP A N   
480  C CA  . ASP A 71  ? 0.9285 0.8723 0.9243 -0.0209 0.0669  -0.0997 250 ASP A CA  
481  C C   . ASP A 71  ? 0.9200 0.8802 0.9199 -0.0149 0.0638  -0.0885 250 ASP A C   
482  O O   . ASP A 71  ? 0.9047 0.8716 0.9118 -0.0079 0.0676  -0.0903 250 ASP A O   
483  C CB  . ASP A 71  ? 0.9433 0.8661 0.9430 -0.0219 0.0629  -0.0945 250 ASP A CB  
484  C CG  . ASP A 71  ? 0.9477 0.8544 0.9621 -0.0109 0.0627  -0.0906 250 ASP A CG  
485  O OD1 . ASP A 71  ? 0.9552 0.8695 0.9791 -0.0016 0.0654  -0.0914 250 ASP A OD1 
486  O OD2 . ASP A 71  ? 0.9406 0.8277 0.9572 -0.0120 0.0597  -0.0863 250 ASP A OD2 
487  N N   . ILE A 72  ? 0.9084 0.8753 0.9041 -0.0180 0.0571  -0.0777 251 ILE A N   
488  C CA  . ILE A 72  ? 0.8849 0.8679 0.8815 -0.0147 0.0539  -0.0682 251 ILE A CA  
489  C C   . ILE A 72  ? 0.8543 0.8311 0.8595 -0.0092 0.0487  -0.0570 251 ILE A C   
490  O O   . ILE A 72  ? 0.7915 0.7761 0.8026 -0.0033 0.0474  -0.0508 251 ILE A O   
491  C CB  . ILE A 72  ? 0.8980 0.8957 0.8827 -0.0223 0.0504  -0.0659 251 ILE A CB  
492  C CG1 . ILE A 72  ? 0.9060 0.9082 0.8800 -0.0298 0.0540  -0.0769 251 ILE A CG1 
493  C CG2 . ILE A 72  ? 0.8840 0.8966 0.8689 -0.0187 0.0478  -0.0575 251 ILE A CG2 
494  C CD1 . ILE A 72  ? 0.8983 0.9138 0.8617 -0.0375 0.0492  -0.0745 251 ILE A CD1 
495  N N   . ARG A 73  ? 0.8411 0.8039 0.8459 -0.0122 0.0460  -0.0545 252 ARG A N   
496  C CA  . ARG A 73  ? 0.8097 0.7701 0.8169 -0.0109 0.0402  -0.0430 252 ARG A CA  
497  C C   . ARG A 73  ? 0.7624 0.7023 0.7710 -0.0129 0.0389  -0.0414 252 ARG A C   
498  O O   . ARG A 73  ? 0.7457 0.6750 0.7503 -0.0187 0.0415  -0.0488 252 ARG A O   
499  C CB  . ARG A 73  ? 0.8333 0.8084 0.8322 -0.0170 0.0368  -0.0388 252 ARG A CB  
500  C CG  . ARG A 73  ? 0.8421 0.8199 0.8320 -0.0265 0.0379  -0.0457 252 ARG A CG  
501  C CD  . ARG A 73  ? 0.8530 0.8500 0.8370 -0.0299 0.0351  -0.0434 252 ARG A CD  
502  N NE  . ARG A 73  ? 0.8632 0.8645 0.8477 -0.0313 0.0306  -0.0353 252 ARG A NE  
503  C CZ  . ARG A 73  ? 0.8905 0.9076 0.8726 -0.0324 0.0275  -0.0321 252 ARG A CZ  
504  N NH1 . ARG A 73  ? 0.9093 0.9385 0.8879 -0.0319 0.0274  -0.0345 252 ARG A NH1 
505  N NH2 . ARG A 73  ? 0.9161 0.9369 0.8994 -0.0338 0.0246  -0.0264 252 ARG A NH2 
506  N N   . GLY A 74  ? 0.7081 0.6422 0.7216 -0.0087 0.0344  -0.0313 253 GLY A N   
507  C CA  . GLY A 74  ? 0.6529 0.5682 0.6658 -0.0116 0.0317  -0.0261 253 GLY A CA  
508  C C   . GLY A 74  ? 0.6052 0.5270 0.6122 -0.0165 0.0269  -0.0159 253 GLY A C   
509  O O   . GLY A 74  ? 0.5983 0.5071 0.6040 -0.0185 0.0237  -0.0084 253 GLY A O   
510  N N   . ASP A 75  ? 0.5625 0.5043 0.5655 -0.0185 0.0265  -0.0158 254 ASP A N   
511  C CA  . ASP A 75  ? 0.5484 0.4996 0.5467 -0.0224 0.0230  -0.0082 254 ASP A CA  
512  C C   . ASP A 75  ? 0.5152 0.4665 0.5058 -0.0335 0.0238  -0.0103 254 ASP A C   
513  O O   . ASP A 75  ? 0.5101 0.4551 0.4987 -0.0384 0.0266  -0.0177 254 ASP A O   
514  C CB  . ASP A 75  ? 0.5660 0.5372 0.5648 -0.0191 0.0223  -0.0080 254 ASP A CB  
515  C CG  . ASP A 75  ? 0.5960 0.5790 0.5907 -0.0231 0.0247  -0.0154 254 ASP A CG  
516  O OD1 . ASP A 75  ? 0.5989 0.5780 0.5938 -0.0231 0.0280  -0.0227 254 ASP A OD1 
517  O OD2 . ASP A 75  ? 0.6299 0.6264 0.6214 -0.0261 0.0231  -0.0139 254 ASP A OD2 
518  N N   . LYS A 76  ? 0.4706 0.4304 0.4573 -0.0379 0.0215  -0.0043 255 LYS A N   
519  C CA  . LYS A 76  ? 0.4472 0.4138 0.4283 -0.0484 0.0224  -0.0064 255 LYS A CA  
520  C C   . LYS A 76  ? 0.4069 0.3936 0.3872 -0.0484 0.0208  -0.0035 255 LYS A C   
521  O O   . LYS A 76  ? 0.3985 0.3874 0.3801 -0.0429 0.0187  0.0024  255 LYS A O   
522  C CB  . LYS A 76  ? 0.4575 0.4065 0.4343 -0.0563 0.0224  -0.0024 255 LYS A CB  
523  C CG  . LYS A 76  ? 0.4704 0.4124 0.4455 -0.0548 0.0193  0.0084  255 LYS A CG  
524  C CD  . LYS A 76  ? 0.4959 0.4164 0.4662 -0.0622 0.0189  0.0134  255 LYS A CD  
525  C CE  . LYS A 76  ? 0.5093 0.4246 0.4754 -0.0622 0.0151  0.0252  255 LYS A CE  
526  N NZ  . LYS A 76  ? 0.5152 0.4271 0.4875 -0.0498 0.0115  0.0296  255 LYS A NZ  
527  N N   . ILE A 77  ? 0.3758 0.3776 0.3549 -0.0542 0.0217  -0.0082 256 ILE A N   
528  C CA  . ILE A 77  ? 0.3579 0.3799 0.3386 -0.0521 0.0205  -0.0074 256 ILE A CA  
529  C C   . ILE A 77  ? 0.3548 0.3885 0.3339 -0.0616 0.0214  -0.0085 256 ILE A C   
530  O O   . ILE A 77  ? 0.3275 0.3562 0.3041 -0.0707 0.0231  -0.0111 256 ILE A O   
531  C CB  . ILE A 77  ? 0.3526 0.3863 0.3363 -0.0464 0.0198  -0.0120 256 ILE A CB  
532  C CG1 . ILE A 77  ? 0.3562 0.3939 0.3382 -0.0524 0.0208  -0.0192 256 ILE A CG1 
533  C CG2 . ILE A 77  ? 0.3509 0.3766 0.3367 -0.0374 0.0194  -0.0105 256 ILE A CG2 
534  C CD1 . ILE A 77  ? 0.3593 0.4133 0.3426 -0.0489 0.0190  -0.0223 256 ILE A CD1 
535  N N   . THR A 78  ? 0.3510 0.4010 0.3325 -0.0593 0.0207  -0.0072 257 THR A N   
536  C CA  . THR A 78  ? 0.3592 0.4269 0.3423 -0.0661 0.0220  -0.0098 257 THR A CA  
537  C C   . THR A 78  ? 0.3522 0.4385 0.3412 -0.0585 0.0204  -0.0113 257 THR A C   
538  O O   . THR A 78  ? 0.3440 0.4274 0.3335 -0.0507 0.0192  -0.0082 257 THR A O   
539  C CB  . THR A 78  ? 0.3728 0.4362 0.3509 -0.0749 0.0242  -0.0055 257 THR A CB  
540  O OG1 . THR A 78  ? 0.4007 0.4837 0.3816 -0.0824 0.0263  -0.0094 257 THR A OG1 
541  C CG2 . THR A 78  ? 0.3735 0.4336 0.3487 -0.0702 0.0235  0.0005  257 THR A CG2 
542  N N   . TRP A 79  ? 0.3287 0.4338 0.3231 -0.0607 0.0202  -0.0162 258 TRP A N   
543  C CA  . TRP A 79  ? 0.3124 0.4351 0.3141 -0.0532 0.0183  -0.0180 258 TRP A CA  
544  C C   . TRP A 79  ? 0.3067 0.4432 0.3117 -0.0558 0.0209  -0.0188 258 TRP A C   
545  O O   . TRP A 79  ? 0.3077 0.4521 0.3128 -0.0655 0.0236  -0.0208 258 TRP A O   
546  C CB  . TRP A 79  ? 0.3097 0.4465 0.3164 -0.0530 0.0155  -0.0225 258 TRP A CB  
547  C CG  . TRP A 79  ? 0.3112 0.4381 0.3142 -0.0490 0.0130  -0.0223 258 TRP A CG  
548  C CD1 . TRP A 79  ? 0.3320 0.4518 0.3302 -0.0550 0.0133  -0.0251 258 TRP A CD1 
549  C CD2 . TRP A 79  ? 0.3146 0.4385 0.3180 -0.0389 0.0104  -0.0197 258 TRP A CD2 
550  N NE1 . TRP A 79  ? 0.3364 0.4501 0.3317 -0.0492 0.0115  -0.0248 258 TRP A NE1 
551  C CE2 . TRP A 79  ? 0.3387 0.4547 0.3369 -0.0397 0.0096  -0.0209 258 TRP A CE2 
552  C CE3 . TRP A 79  ? 0.3138 0.4401 0.3210 -0.0300 0.0089  -0.0169 258 TRP A CE3 
553  C CZ2 . TRP A 79  ? 0.3356 0.4475 0.3320 -0.0324 0.0076  -0.0187 258 TRP A CZ2 
554  C CZ3 . TRP A 79  ? 0.3176 0.4381 0.3233 -0.0230 0.0065  -0.0144 258 TRP A CZ3 
555  C CH2 . TRP A 79  ? 0.3269 0.4409 0.3272 -0.0244 0.0060  -0.0149 258 TRP A CH2 
556  N N   . ILE A 80  ? 0.2999 0.4394 0.3074 -0.0476 0.0204  -0.0179 259 ILE A N   
557  C CA  . ILE A 80  ? 0.3095 0.4617 0.3196 -0.0493 0.0236  -0.0198 259 ILE A CA  
558  C C   . ILE A 80  ? 0.3164 0.4850 0.3373 -0.0398 0.0220  -0.0241 259 ILE A C   
559  O O   . ILE A 80  ? 0.3194 0.4812 0.3416 -0.0304 0.0188  -0.0226 259 ILE A O   
560  C CB  . ILE A 80  ? 0.3090 0.4476 0.3103 -0.0498 0.0251  -0.0152 259 ILE A CB  
561  C CG1 . ILE A 80  ? 0.3292 0.4509 0.3206 -0.0586 0.0260  -0.0100 259 ILE A CG1 
562  C CG2 . ILE A 80  ? 0.3076 0.4602 0.3104 -0.0508 0.0287  -0.0183 259 ILE A CG2 
563  C CD1 . ILE A 80  ? 0.3265 0.4554 0.3162 -0.0712 0.0296  -0.0113 259 ILE A CD1 
564  N N   . GLU A 81  ? 0.3105 0.5008 0.3399 -0.0426 0.0243  -0.0294 260 GLU A N   
565  C CA  . GLU A 81  ? 0.3161 0.5239 0.3584 -0.0332 0.0228  -0.0342 260 GLU A CA  
566  C C   . GLU A 81  ? 0.3059 0.5133 0.3484 -0.0283 0.0258  -0.0361 260 GLU A C   
567  O O   . GLU A 81  ? 0.2971 0.5061 0.3466 -0.0175 0.0234  -0.0380 260 GLU A O   
568  C CB  . GLU A 81  ? 0.3341 0.5673 0.3874 -0.0381 0.0241  -0.0398 260 GLU A CB  
569  C CG  . GLU A 81  ? 0.3516 0.6038 0.4208 -0.0271 0.0210  -0.0443 260 GLU A CG  
570  C CD  . GLU A 81  ? 0.3662 0.6299 0.4436 -0.0213 0.0251  -0.0498 260 GLU A CD  
571  O OE1 . GLU A 81  ? 0.3701 0.6330 0.4408 -0.0285 0.0315  -0.0513 260 GLU A OE1 
572  O OE2 . GLU A 81  ? 0.3697 0.6424 0.4598 -0.0094 0.0219  -0.0527 260 GLU A OE2 
573  N N   . GLY A 82  ? 0.3113 0.5161 0.3452 -0.0368 0.0308  -0.0356 261 GLY A N   
574  C CA  . GLY A 82  ? 0.3141 0.5169 0.3446 -0.0340 0.0337  -0.0374 261 GLY A CA  
575  C C   . GLY A 82  ? 0.3166 0.5390 0.3493 -0.0406 0.0406  -0.0437 261 GLY A C   
576  O O   . GLY A 82  ? 0.3154 0.5358 0.3411 -0.0423 0.0441  -0.0449 261 GLY A O   
577  N N   . LYS A 83  ? 0.3323 0.5750 0.3747 -0.0450 0.0427  -0.0479 262 LYS A N   
578  C CA  . LYS A 83  ? 0.3502 0.6159 0.3976 -0.0508 0.0500  -0.0551 262 LYS A CA  
579  C C   . LYS A 83  ? 0.3507 0.6186 0.3886 -0.0676 0.0543  -0.0519 262 LYS A C   
580  O O   . LYS A 83  ? 0.3386 0.6259 0.3786 -0.0756 0.0613  -0.0570 262 LYS A O   
581  C CB  . LYS A 83  ? 0.3675 0.6589 0.4357 -0.0433 0.0499  -0.0634 262 LYS A CB  
582  C CG  . LYS A 83  ? 0.3993 0.6889 0.4783 -0.0265 0.0456  -0.0666 262 LYS A CG  
583  C CD  . LYS A 83  ? 0.4113 0.7267 0.5121 -0.0184 0.0446  -0.0738 262 LYS A CD  
584  C CE  . LYS A 83  ? 0.4506 0.7588 0.5612 -0.0020 0.0373  -0.0733 262 LYS A CE  
585  N NZ  . LYS A 83  ? 0.4837 0.7768 0.5899 0.0056  0.0387  -0.0753 262 LYS A NZ  
586  N N   . GLU A 84  ? 0.3408 0.5886 0.3686 -0.0732 0.0506  -0.0437 263 GLU A N   
587  C CA  . GLU A 84  ? 0.3284 0.5733 0.3465 -0.0891 0.0539  -0.0397 263 GLU A CA  
588  C C   . GLU A 84  ? 0.3318 0.5728 0.3360 -0.0973 0.0591  -0.0370 263 GLU A C   
589  O O   . GLU A 84  ? 0.3500 0.5792 0.3471 -0.0911 0.0576  -0.0348 263 GLU A O   
590  C CB  . GLU A 84  ? 0.3295 0.5493 0.3390 -0.0917 0.0487  -0.0318 263 GLU A CB  
591  C CG  . GLU A 84  ? 0.3185 0.5405 0.3383 -0.0854 0.0435  -0.0340 263 GLU A CG  
592  C CD  . GLU A 84  ? 0.3176 0.5296 0.3405 -0.0702 0.0378  -0.0331 263 GLU A CD  
593  O OE1 . GLU A 84  ? 0.3082 0.5160 0.3290 -0.0632 0.0383  -0.0328 263 GLU A OE1 
594  O OE2 . GLU A 84  ? 0.3184 0.5265 0.3448 -0.0665 0.0332  -0.0326 263 GLU A OE2 
595  N N   . PRO A 85  ? 0.3273 0.5785 0.3263 -0.1126 0.0651  -0.0368 264 PRO A N   
596  C CA  . PRO A 85  ? 0.3227 0.5679 0.3048 -0.1228 0.0695  -0.0320 264 PRO A CA  
597  C C   . PRO A 85  ? 0.3329 0.5458 0.2996 -0.1223 0.0636  -0.0206 264 PRO A C   
598  O O   . PRO A 85  ? 0.3447 0.5405 0.3097 -0.1243 0.0594  -0.0150 264 PRO A O   
599  C CB  . PRO A 85  ? 0.3250 0.5819 0.3044 -0.1405 0.0753  -0.0314 264 PRO A CB  
600  C CG  . PRO A 85  ? 0.3150 0.5971 0.3151 -0.1374 0.0763  -0.0410 264 PRO A CG  
601  C CD  . PRO A 85  ? 0.3095 0.5795 0.3181 -0.1217 0.0679  -0.0408 264 PRO A CD  
602  N N   . GLY A 86  ? 0.3301 0.5355 0.2865 -0.1191 0.0631  -0.0180 265 GLY A N   
603  C CA  . GLY A 86  ? 0.3537 0.5315 0.2965 -0.1182 0.0572  -0.0072 265 GLY A CA  
604  C C   . GLY A 86  ? 0.3596 0.5247 0.3095 -0.1026 0.0504  -0.0072 265 GLY A C   
605  O O   . GLY A 86  ? 0.3714 0.5152 0.3133 -0.1002 0.0451  0.0010  265 GLY A O   
606  N N   . CYS A 87  ? 0.3517 0.5304 0.3170 -0.0923 0.0504  -0.0161 266 CYS A N   
607  C CA  . CYS A 87  ? 0.3445 0.5126 0.3169 -0.0786 0.0445  -0.0162 266 CYS A CA  
608  C C   . CYS A 87  ? 0.3449 0.5242 0.3246 -0.0684 0.0454  -0.0240 266 CYS A C   
609  O O   . CYS A 87  ? 0.3401 0.5154 0.3284 -0.0572 0.0414  -0.0258 266 CYS A O   
610  C CB  . CYS A 87  ? 0.3361 0.5061 0.3197 -0.0754 0.0422  -0.0181 266 CYS A CB  
611  S SG  . CYS A 87  ? 0.3529 0.5056 0.3292 -0.0858 0.0407  -0.0107 266 CYS A SG  
612  N N   . GLU A 88  ? 0.3471 0.5394 0.3225 -0.0730 0.0508  -0.0286 267 GLU A N   
613  C CA  . GLU A 88  ? 0.3495 0.5540 0.3325 -0.0645 0.0531  -0.0381 267 GLU A CA  
614  C C   . GLU A 88  ? 0.3332 0.5209 0.3131 -0.0553 0.0477  -0.0359 267 GLU A C   
615  O O   . GLU A 88  ? 0.3161 0.5065 0.3063 -0.0446 0.0467  -0.0422 267 GLU A O   
616  C CB  . GLU A 88  ? 0.3763 0.5976 0.3529 -0.0730 0.0609  -0.0440 267 GLU A CB  
617  C CG  . GLU A 88  ? 0.4106 0.6531 0.3930 -0.0821 0.0673  -0.0480 267 GLU A CG  
618  C CD  . GLU A 88  ? 0.4463 0.6826 0.4149 -0.0977 0.0686  -0.0388 267 GLU A CD  
619  O OE1 . GLU A 88  ? 0.4650 0.6782 0.4245 -0.0989 0.0626  -0.0283 267 GLU A OE1 
620  O OE2 . GLU A 88  ? 0.4580 0.7127 0.4259 -0.1088 0.0758  -0.0423 267 GLU A OE2 
621  N N   . THR A 89  ? 0.3322 0.5025 0.2984 -0.0597 0.0441  -0.0268 268 THR A N   
622  C CA  . THR A 89  ? 0.3269 0.4834 0.2900 -0.0527 0.0392  -0.0246 268 THR A CA  
623  C C   . THR A 89  ? 0.3149 0.4601 0.2877 -0.0432 0.0337  -0.0219 268 THR A C   
624  O O   . THR A 89  ? 0.2956 0.4355 0.2728 -0.0347 0.0309  -0.0241 268 THR A O   
625  C CB  . THR A 89  ? 0.3443 0.4896 0.2907 -0.0603 0.0367  -0.0162 268 THR A CB  
626  O OG1 . THR A 89  ? 0.3549 0.5117 0.2912 -0.0716 0.0424  -0.0173 268 THR A OG1 
627  C CG2 . THR A 89  ? 0.3561 0.4947 0.2986 -0.0554 0.0333  -0.0171 268 THR A CG2 
628  N N   . ILE A 90  ? 0.3040 0.4454 0.2792 -0.0455 0.0324  -0.0174 269 ILE A N   
629  C CA  . ILE A 90  ? 0.3035 0.4376 0.2874 -0.0376 0.0283  -0.0160 269 ILE A CA  
630  C C   . ILE A 90  ? 0.3009 0.4477 0.2978 -0.0294 0.0292  -0.0240 269 ILE A C   
631  O O   . ILE A 90  ? 0.2983 0.4386 0.3007 -0.0207 0.0255  -0.0239 269 ILE A O   
632  C CB  . ILE A 90  ? 0.3035 0.4326 0.2867 -0.0429 0.0277  -0.0114 269 ILE A CB  
633  C CG1 . ILE A 90  ? 0.3088 0.4222 0.2804 -0.0494 0.0260  -0.0029 269 ILE A CG1 
634  C CG2 . ILE A 90  ? 0.2969 0.4216 0.2884 -0.0355 0.0241  -0.0115 269 ILE A CG2 
635  C CD1 . ILE A 90  ? 0.3081 0.4163 0.2775 -0.0571 0.0268  0.0006  269 ILE A CD1 
636  N N   . GLY A 91  ? 0.2965 0.4616 0.2982 -0.0322 0.0340  -0.0306 270 GLY A N   
637  C CA  . GLY A 91  ? 0.2878 0.4669 0.3034 -0.0238 0.0349  -0.0388 270 GLY A CA  
638  C C   . GLY A 91  ? 0.2916 0.4649 0.3089 -0.0152 0.0339  -0.0426 270 GLY A C   
639  O O   . GLY A 91  ? 0.2962 0.4681 0.3235 -0.0053 0.0308  -0.0446 270 GLY A O   
640  N N   . LEU A 92  ? 0.2938 0.4631 0.3005 -0.0197 0.0361  -0.0432 271 LEU A N   
641  C CA  . LEU A 92  ? 0.3045 0.4675 0.3109 -0.0137 0.0354  -0.0477 271 LEU A CA  
642  C C   . LEU A 92  ? 0.3006 0.4448 0.3060 -0.0083 0.0290  -0.0411 271 LEU A C   
643  O O   . LEU A 92  ? 0.3088 0.4477 0.3207 -0.0002 0.0270  -0.0443 271 LEU A O   
644  C CB  . LEU A 92  ? 0.3227 0.4878 0.3160 -0.0218 0.0392  -0.0499 271 LEU A CB  
645  C CG  . LEU A 92  ? 0.3509 0.5069 0.3402 -0.0183 0.0377  -0.0535 271 LEU A CG  
646  C CD1 . LEU A 92  ? 0.3566 0.5189 0.3582 -0.0091 0.0405  -0.0651 271 LEU A CD1 
647  C CD2 . LEU A 92  ? 0.3625 0.5201 0.3356 -0.0283 0.0401  -0.0535 271 LEU A CD2 
648  N N   . LEU A 93  ? 0.2944 0.4285 0.2923 -0.0131 0.0260  -0.0320 272 LEU A N   
649  C CA  . LEU A 93  ? 0.2908 0.4096 0.2889 -0.0087 0.0207  -0.0260 272 LEU A CA  
650  C C   . LEU A 93  ? 0.2887 0.4080 0.2980 -0.0004 0.0185  -0.0270 272 LEU A C   
651  O O   . LEU A 93  ? 0.3026 0.4131 0.3151 0.0056  0.0156  -0.0265 272 LEU A O   
652  C CB  . LEU A 93  ? 0.2848 0.3953 0.2759 -0.0143 0.0186  -0.0173 272 LEU A CB  
653  C CG  . LEU A 93  ? 0.2830 0.3814 0.2768 -0.0098 0.0144  -0.0118 272 LEU A CG  
654  C CD1 . LEU A 93  ? 0.2803 0.3697 0.2722 -0.0072 0.0115  -0.0105 272 LEU A CD1 
655  C CD2 . LEU A 93  ? 0.2788 0.3711 0.2685 -0.0144 0.0135  -0.0055 272 LEU A CD2 
656  N N   . MET A 94  ? 0.2883 0.4182 0.3031 -0.0011 0.0197  -0.0280 273 MET A N   
657  C CA  . MET A 94  ? 0.2857 0.4178 0.3099 0.0056  0.0167  -0.0277 273 MET A CA  
658  C C   . MET A 94  ? 0.2739 0.4097 0.3076 0.0146  0.0164  -0.0336 273 MET A C   
659  O O   . MET A 94  ? 0.2599 0.3884 0.2981 0.0215  0.0123  -0.0313 273 MET A O   
660  C CB  . MET A 94  ? 0.2878 0.4333 0.3158 0.0017  0.0180  -0.0284 273 MET A CB  
661  C CG  . MET A 94  ? 0.2986 0.4365 0.3189 -0.0054 0.0172  -0.0222 273 MET A CG  
662  S SD  . MET A 94  ? 0.3091 0.4621 0.3314 -0.0139 0.0201  -0.0243 273 MET A SD  
663  C CE  . MET A 94  ? 0.2990 0.4601 0.3318 -0.0071 0.0155  -0.0252 273 MET A CE  
664  N N   . SER A 95  ? 0.2700 0.4162 0.3062 0.0142  0.0208  -0.0414 274 SER A N   
665  C CA  . SER A 95  ? 0.2786 0.4273 0.3249 0.0233  0.0211  -0.0485 274 SER A CA  
666  C C   . SER A 95  ? 0.2827 0.4135 0.3243 0.0262  0.0190  -0.0478 274 SER A C   
667  O O   . SER A 95  ? 0.2873 0.4120 0.3368 0.0348  0.0166  -0.0499 274 SER A O   
668  C CB  . SER A 95  ? 0.2963 0.4626 0.3475 0.0222  0.0274  -0.0586 274 SER A CB  
669  O OG  . SER A 95  ? 0.3340 0.4979 0.3734 0.0147  0.0315  -0.0611 274 SER A OG  
670  N N   . SER A 96  ? 0.2850 0.4072 0.3143 0.0189  0.0194  -0.0444 275 SER A N   
671  C CA  . SER A 96  ? 0.2947 0.4017 0.3192 0.0198  0.0172  -0.0437 275 SER A CA  
672  C C   . SER A 96  ? 0.2959 0.3901 0.3224 0.0236  0.0119  -0.0359 275 SER A C   
673  O O   . SER A 96  ? 0.2887 0.3717 0.3176 0.0280  0.0097  -0.0364 275 SER A O   
674  C CB  . SER A 96  ? 0.3046 0.4092 0.3166 0.0109  0.0182  -0.0417 275 SER A CB  
675  O OG  . SER A 96  ? 0.3096 0.4267 0.3177 0.0060  0.0234  -0.0482 275 SER A OG  
676  N N   . MET A 97  ? 0.2947 0.3904 0.3195 0.0212  0.0103  -0.0290 276 MET A N   
677  C CA  . MET A 97  ? 0.3023 0.3891 0.3283 0.0240  0.0062  -0.0220 276 MET A CA  
678  C C   . MET A 97  ? 0.2997 0.3866 0.3350 0.0325  0.0037  -0.0234 276 MET A C   
679  O O   . MET A 97  ? 0.3130 0.3879 0.3489 0.0360  0.0005  -0.0198 276 MET A O   
680  C CB  . MET A 97  ? 0.3022 0.3936 0.3256 0.0199  0.0059  -0.0171 276 MET A CB  
681  C CG  . MET A 97  ? 0.3157 0.4019 0.3307 0.0132  0.0067  -0.0131 276 MET A CG  
682  S SD  . MET A 97  ? 0.3456 0.4357 0.3589 0.0092  0.0069  -0.0092 276 MET A SD  
683  C CE  . MET A 97  ? 0.3456 0.4275 0.3509 0.0030  0.0074  -0.0049 276 MET A CE  
684  N N   . ASP A 98  ? 0.2940 0.3949 0.3370 0.0356  0.0050  -0.0281 277 ASP A N   
685  C CA  . ASP A 98  ? 0.3004 0.4044 0.3545 0.0448  0.0020  -0.0294 277 ASP A CA  
686  C C   . ASP A 98  ? 0.3107 0.4027 0.3686 0.0511  0.0014  -0.0332 277 ASP A C   
687  O O   . ASP A 98  ? 0.3106 0.3930 0.3728 0.0576  -0.0032 -0.0293 277 ASP A O   
688  C CB  . ASP A 98  ? 0.2925 0.4170 0.3559 0.0465  0.0042  -0.0352 277 ASP A CB  
689  C CG  . ASP A 98  ? 0.2989 0.4342 0.3600 0.0408  0.0036  -0.0311 277 ASP A CG  
690  O OD1 . ASP A 98  ? 0.3104 0.4365 0.3637 0.0374  0.0009  -0.0239 277 ASP A OD1 
691  O OD2 . ASP A 98  ? 0.3033 0.4564 0.3706 0.0393  0.0061  -0.0360 277 ASP A OD2 
692  N N   . ASP A 99  ? 0.3255 0.4175 0.3809 0.0485  0.0059  -0.0408 278 ASP A N   
693  C CA  . ASP A 99  ? 0.3434 0.4242 0.4019 0.0532  0.0063  -0.0468 278 ASP A CA  
694  C C   . ASP A 99  ? 0.3437 0.4040 0.3968 0.0525  0.0022  -0.0398 278 ASP A C   
695  O O   . ASP A 99  ? 0.3428 0.3909 0.4016 0.0592  -0.0007 -0.0399 278 ASP A O   
696  C CB  . ASP A 99  ? 0.3685 0.4540 0.4218 0.0479  0.0121  -0.0562 278 ASP A CB  
697  C CG  . ASP A 99  ? 0.3992 0.5049 0.4591 0.0490  0.0174  -0.0651 278 ASP A CG  
698  O OD1 . ASP A 99  ? 0.4179 0.5343 0.4890 0.0553  0.0162  -0.0651 278 ASP A OD1 
699  O OD2 . ASP A 99  ? 0.4246 0.5366 0.4781 0.0430  0.0226  -0.0720 278 ASP A OD2 
700  N N   . LEU A 100 ? 0.3181 0.3749 0.3610 0.0443  0.0019  -0.0337 279 LEU A N   
701  C CA  . LEU A 100 ? 0.3291 0.3699 0.3672 0.0421  -0.0013 -0.0269 279 LEU A CA  
702  C C   . LEU A 100 ? 0.3308 0.3656 0.3728 0.0475  -0.0058 -0.0194 279 LEU A C   
703  O O   . LEU A 100 ? 0.3464 0.3663 0.3896 0.0502  -0.0086 -0.0169 279 LEU A O   
704  C CB  . LEU A 100 ? 0.3285 0.3713 0.3576 0.0335  -0.0006 -0.0217 279 LEU A CB  
705  C CG  . LEU A 100 ? 0.3214 0.3659 0.3443 0.0272  0.0019  -0.0264 279 LEU A CG  
706  C CD1 . LEU A 100 ? 0.3112 0.3555 0.3277 0.0206  0.0010  -0.0197 279 LEU A CD1 
707  C CD2 . LEU A 100 ? 0.3239 0.3572 0.3471 0.0276  0.0017  -0.0320 279 LEU A CD2 
708  N N   . ILE A 101 ? 0.3263 0.3726 0.3695 0.0482  -0.0068 -0.0154 280 ILE A N   
709  C CA  . ILE A 101 ? 0.3333 0.3767 0.3779 0.0520  -0.0116 -0.0076 280 ILE A CA  
710  C C   . ILE A 101 ? 0.3397 0.3780 0.3941 0.0619  -0.0150 -0.0091 280 ILE A C   
711  O O   . ILE A 101 ? 0.3540 0.3793 0.4077 0.0647  -0.0195 -0.0022 280 ILE A O   
712  C CB  . ILE A 101 ? 0.3286 0.3871 0.3721 0.0498  -0.0118 -0.0049 280 ILE A CB  
713  C CG1 . ILE A 101 ? 0.3253 0.3835 0.3593 0.0410  -0.0095 -0.0014 280 ILE A CG1 
714  C CG2 . ILE A 101 ? 0.3224 0.3823 0.3690 0.0550  -0.0173 0.0013  280 ILE A CG2 
715  C CD1 . ILE A 101 ? 0.3338 0.3795 0.3616 0.0384  -0.0113 0.0060  280 ILE A CD1 
716  N N   . ARG A 102 ? 0.3421 0.3906 0.4057 0.0671  -0.0128 -0.0182 281 ARG A N   
717  C CA  . ARG A 102 ? 0.3597 0.4045 0.4353 0.0781  -0.0156 -0.0213 281 ARG A CA  
718  C C   . ARG A 102 ? 0.3675 0.3886 0.4415 0.0798  -0.0172 -0.0205 281 ARG A C   
719  O O   . ARG A 102 ? 0.3599 0.3695 0.4393 0.0874  -0.0224 -0.0159 281 ARG A O   
720  C CB  . ARG A 102 ? 0.3812 0.4420 0.4671 0.0824  -0.0110 -0.0335 281 ARG A CB  
721  C CG  . ARG A 102 ? 0.4216 0.5051 0.5159 0.0853  -0.0119 -0.0338 281 ARG A CG  
722  C CD  . ARG A 102 ? 0.4518 0.5512 0.5597 0.0914  -0.0076 -0.0460 281 ARG A CD  
723  N NE  . ARG A 102 ? 0.4910 0.6026 0.5934 0.0827  0.0003  -0.0539 281 ARG A NE  
724  C CZ  . ARG A 102 ? 0.5238 0.6530 0.6231 0.0754  0.0028  -0.0533 281 ARG A CZ  
725  N NH1 . ARG A 102 ? 0.5325 0.6713 0.6351 0.0761  -0.0017 -0.0468 281 ARG A NH1 
726  N NH2 . ARG A 102 ? 0.5326 0.6694 0.6249 0.0669  0.0095  -0.0590 281 ARG A NH2 
727  N N   . HIS A 103 ? 0.3764 0.3900 0.4427 0.0724  -0.0131 -0.0245 282 HIS A N   
728  C CA  . HIS A 103 ? 0.3999 0.3916 0.4643 0.0720  -0.0140 -0.0253 282 HIS A CA  
729  C C   . HIS A 103 ? 0.4194 0.3971 0.4757 0.0672  -0.0180 -0.0129 282 HIS A C   
730  O O   . HIS A 103 ? 0.4445 0.4024 0.4999 0.0671  -0.0199 -0.0110 282 HIS A O   
731  C CB  . HIS A 103 ? 0.3979 0.3892 0.4576 0.0655  -0.0086 -0.0351 282 HIS A CB  
732  C CG  . HIS A 103 ? 0.4042 0.4055 0.4715 0.0706  -0.0042 -0.0483 282 HIS A CG  
733  N ND1 . HIS A 103 ? 0.4042 0.3981 0.4830 0.0810  -0.0049 -0.0549 282 HIS A ND1 
734  C CD2 . HIS A 103 ? 0.3964 0.4144 0.4613 0.0664  0.0012  -0.0564 282 HIS A CD2 
735  C CE1 . HIS A 103 ? 0.3936 0.4013 0.4776 0.0832  0.0007  -0.0676 282 HIS A CE1 
736  N NE2 . HIS A 103 ? 0.3920 0.4145 0.4667 0.0738  0.0045  -0.0683 282 HIS A NE2 
737  N N   . CYS A 104 ? 0.4275 0.4154 0.4779 0.0626  -0.0188 -0.0051 283 CYS A N   
738  C CA  . CYS A 104 ? 0.4575 0.4358 0.5000 0.0576  -0.0217 0.0062  283 CYS A CA  
739  C C   . CYS A 104 ? 0.4916 0.4662 0.5369 0.0645  -0.0278 0.0147  283 CYS A C   
740  O O   . CYS A 104 ? 0.5210 0.4794 0.5620 0.0633  -0.0312 0.0230  283 CYS A O   
741  C CB  . CYS A 104 ? 0.4369 0.4282 0.4719 0.0499  -0.0194 0.0097  283 CYS A CB  
742  S SG  . CYS A 104 ? 0.4259 0.4199 0.4559 0.0407  -0.0141 0.0040  283 CYS A SG  
743  N N   . ASN A 105 ? 0.5073 0.4977 0.5593 0.0709  -0.0294 0.0130  284 ASN A N   
744  C CA  . ASN A 105 ? 0.5180 0.5114 0.5713 0.0761  -0.0358 0.0218  284 ASN A CA  
745  C C   . ASN A 105 ? 0.5100 0.4816 0.5639 0.0809  -0.0416 0.0295  284 ASN A C   
746  O O   . ASN A 105 ? 0.4960 0.4546 0.5575 0.0869  -0.0418 0.0244  284 ASN A O   
747  C CB  . ASN A 105 ? 0.5455 0.5586 0.6103 0.0840  -0.0370 0.0164  284 ASN A CB  
748  C CG  . ASN A 105 ? 0.5655 0.5852 0.6312 0.0884  -0.0445 0.0257  284 ASN A CG  
749  O OD1 . ASN A 105 ? 0.5789 0.6020 0.6338 0.0815  -0.0458 0.0332  284 ASN A OD1 
750  N ND2 . ASN A 105 ? 0.5634 0.5852 0.6422 0.1000  -0.0497 0.0252  284 ASN A ND2 
751  N N   . GLY A 106 ? 0.5028 0.4699 0.5476 0.0777  -0.0461 0.0418  285 GLY A N   
752  C CA  . GLY A 106 ? 0.5041 0.4494 0.5461 0.0802  -0.0521 0.0520  285 GLY A CA  
753  C C   . GLY A 106 ? 0.5143 0.4425 0.5451 0.0694  -0.0489 0.0562  285 GLY A C   
754  O O   . GLY A 106 ? 0.5437 0.4532 0.5692 0.0683  -0.0532 0.0663  285 GLY A O   
755  N N   . LYS A 107 ? 0.4882 0.4235 0.5158 0.0612  -0.0417 0.0490  286 LYS A N   
756  C CA  . LYS A 107 ? 0.4996 0.4223 0.5193 0.0508  -0.0384 0.0512  286 LYS A CA  
757  C C   . LYS A 107 ? 0.4936 0.4308 0.5046 0.0411  -0.0339 0.0529  286 LYS A C   
758  O O   . LYS A 107 ? 0.5036 0.4345 0.5081 0.0320  -0.0312 0.0563  286 LYS A O   
759  C CB  . LYS A 107 ? 0.4980 0.4120 0.5236 0.0506  -0.0347 0.0404  286 LYS A CB  
760  C CG  . LYS A 107 ? 0.5175 0.4129 0.5514 0.0596  -0.0383 0.0380  286 LYS A CG  
761  C CD  . LYS A 107 ? 0.5195 0.4134 0.5604 0.0611  -0.0340 0.0237  286 LYS A CD  
762  C CE  . LYS A 107 ? 0.5246 0.4004 0.5751 0.0711  -0.0368 0.0192  286 LYS A CE  
763  N NZ  . LYS A 107 ? 0.5400 0.3877 0.5860 0.0668  -0.0395 0.0258  286 LYS A NZ  
764  N N   . LEU A 108 ? 0.4906 0.4476 0.5026 0.0430  -0.0330 0.0501  287 LEU A N   
765  C CA  . LEU A 108 ? 0.5079 0.4779 0.5124 0.0352  -0.0292 0.0515  287 LEU A CA  
766  C C   . LEU A 108 ? 0.5202 0.4904 0.5154 0.0329  -0.0327 0.0623  287 LEU A C   
767  O O   . LEU A 108 ? 0.5152 0.4963 0.5102 0.0369  -0.0360 0.0639  287 LEU A O   
768  C CB  . LEU A 108 ? 0.4963 0.4850 0.5054 0.0375  -0.0267 0.0434  287 LEU A CB  
769  C CG  . LEU A 108 ? 0.5073 0.4988 0.5217 0.0366  -0.0221 0.0335  287 LEU A CG  
770  C CD1 . LEU A 108 ? 0.4941 0.5031 0.5112 0.0376  -0.0198 0.0275  287 LEU A CD1 
771  C CD2 . LEU A 108 ? 0.5073 0.4944 0.5173 0.0281  -0.0182 0.0338  287 LEU A CD2 
772  N N   . GLY A 109 ? 0.5415 0.5005 0.5287 0.0255  -0.0319 0.0695  288 GLY A N   
773  C CA  . GLY A 109 ? 0.5608 0.5176 0.5369 0.0220  -0.0352 0.0808  288 GLY A CA  
774  C C   . GLY A 109 ? 0.5690 0.5183 0.5468 0.0309  -0.0439 0.0876  288 GLY A C   
775  O O   . GLY A 109 ? 0.5757 0.5096 0.5606 0.0369  -0.0471 0.0876  288 GLY A O   
776  N N   . SER A 110 ? 0.5817 0.5425 0.5536 0.0319  -0.0478 0.0928  289 SER A N   
777  C CA  . SER A 110 ? 0.5871 0.5449 0.5611 0.0408  -0.0573 0.1000  289 SER A CA  
778  C C   . SER A 110 ? 0.5671 0.5452 0.5504 0.0481  -0.0591 0.0926  289 SER A C   
779  O O   . SER A 110 ? 0.5556 0.5393 0.5401 0.0543  -0.0670 0.0981  289 SER A O   
780  C CB  . SER A 110 ? 0.6181 0.5725 0.5766 0.0352  -0.0620 0.1139  289 SER A CB  
781  O OG  . SER A 110 ? 0.6322 0.6051 0.5808 0.0276  -0.0582 0.1123  289 SER A OG  
782  N N   . TYR A 111 ? 0.5380 0.5271 0.5277 0.0470  -0.0522 0.0805  290 TYR A N   
783  C CA  . TYR A 111 ? 0.5175 0.5265 0.5150 0.0513  -0.0524 0.0728  290 TYR A CA  
784  C C   . TYR A 111 ? 0.5056 0.5143 0.5189 0.0631  -0.0563 0.0684  290 TYR A C   
785  O O   . TYR A 111 ? 0.4974 0.4908 0.5168 0.0671  -0.0557 0.0666  290 TYR A O   
786  C CB  . TYR A 111 ? 0.5088 0.5279 0.5067 0.0452  -0.0437 0.0627  290 TYR A CB  
787  C CG  . TYR A 111 ? 0.5160 0.5395 0.5011 0.0350  -0.0393 0.0647  290 TYR A CG  
788  C CD1 . TYR A 111 ? 0.5094 0.5429 0.4855 0.0320  -0.0424 0.0693  290 TYR A CD1 
789  C CD2 . TYR A 111 ? 0.5194 0.5385 0.5022 0.0285  -0.0322 0.0612  290 TYR A CD2 
790  C CE1 . TYR A 111 ? 0.5070 0.5450 0.4716 0.0228  -0.0375 0.0696  290 TYR A CE1 
791  C CE2 . TYR A 111 ? 0.5187 0.5428 0.4918 0.0202  -0.0276 0.0619  290 TYR A CE2 
792  C CZ  . TYR A 111 ? 0.5154 0.5487 0.4793 0.0173  -0.0298 0.0656  290 TYR A CZ  
793  O OH  . TYR A 111 ? 0.5309 0.5695 0.4855 0.0092  -0.0243 0.0648  290 TYR A OH  
794  N N   . LYS A 112 ? 0.4936 0.5205 0.5138 0.0683  -0.0600 0.0660  291 LYS A N   
795  C CA  . LYS A 112 ? 0.4928 0.5265 0.5301 0.0791  -0.0619 0.0589  291 LYS A CA  
796  C C   . LYS A 112 ? 0.4673 0.5232 0.5096 0.0764  -0.0569 0.0486  291 LYS A C   
797  O O   . LYS A 112 ? 0.4317 0.5046 0.4730 0.0751  -0.0600 0.0498  291 LYS A O   
798  C CB  . LYS A 112 ? 0.5164 0.5516 0.5601 0.0890  -0.0726 0.0671  291 LYS A CB  
799  C CG  . LYS A 112 ? 0.5709 0.5820 0.6086 0.0914  -0.0787 0.0792  291 LYS A CG  
800  C CD  . LYS A 112 ? 0.6067 0.5962 0.6513 0.0957  -0.0757 0.0752  291 LYS A CD  
801  C CE  . LYS A 112 ? 0.6390 0.6027 0.6775 0.0972  -0.0819 0.0878  291 LYS A CE  
802  N NZ  . LYS A 112 ? 0.6632 0.6050 0.7084 0.1004  -0.0786 0.0825  291 LYS A NZ  
803  N N   . ILE A 113 ? 0.4691 0.5242 0.5155 0.0746  -0.0493 0.0388  292 ILE A N   
804  C CA  . ILE A 113 ? 0.4636 0.5365 0.5133 0.0707  -0.0437 0.0296  292 ILE A CA  
805  C C   . ILE A 113 ? 0.4457 0.5349 0.5115 0.0795  -0.0463 0.0238  292 ILE A C   
806  O O   . ILE A 113 ? 0.4621 0.5456 0.5387 0.0880  -0.0469 0.0203  292 ILE A O   
807  C CB  . ILE A 113 ? 0.4794 0.5454 0.5270 0.0656  -0.0356 0.0225  292 ILE A CB  
808  C CG1 . ILE A 113 ? 0.5012 0.5498 0.5372 0.0592  -0.0337 0.0278  292 ILE A CG1 
809  C CG2 . ILE A 113 ? 0.4784 0.5603 0.5259 0.0597  -0.0302 0.0154  292 ILE A CG2 
810  C CD1 . ILE A 113 ? 0.5017 0.5544 0.5261 0.0503  -0.0318 0.0316  292 ILE A CD1 
811  N N   . ASN A 114 ? 0.4312 0.5410 0.4990 0.0769  -0.0472 0.0219  293 ASN A N   
812  C CA  . ASN A 114 ? 0.4328 0.5620 0.5170 0.0845  -0.0496 0.0163  293 ASN A CA  
813  C C   . ASN A 114 ? 0.4101 0.5587 0.4963 0.0771  -0.0435 0.0077  293 ASN A C   
814  O O   . ASN A 114 ? 0.4106 0.5787 0.5108 0.0813  -0.0439 0.0017  293 ASN A O   
815  C CB  . ASN A 114 ? 0.4332 0.5705 0.5222 0.0912  -0.0601 0.0242  293 ASN A CB  
816  C CG  . ASN A 114 ? 0.4444 0.5944 0.5233 0.0828  -0.0632 0.0285  293 ASN A CG  
817  O OD1 . ASN A 114 ? 0.4442 0.6100 0.5294 0.0867  -0.0709 0.0315  293 ASN A OD1 
818  N ND2 . ASN A 114 ? 0.4525 0.5966 0.5164 0.0714  -0.0574 0.0281  293 ASN A ND2 
819  N N   . GLY A 115 ? 0.3831 0.5265 0.4560 0.0663  -0.0379 0.0073  294 GLY A N   
820  C CA  . GLY A 115 ? 0.3402 0.4980 0.4130 0.0582  -0.0323 0.0004  294 GLY A CA  
821  C C   . GLY A 115 ? 0.3257 0.4719 0.3840 0.0480  -0.0267 0.0011  294 GLY A C   
822  O O   . GLY A 115 ? 0.3202 0.4494 0.3695 0.0472  -0.0269 0.0062  294 GLY A O   
823  N N   . ARG A 116 ? 0.3026 0.4584 0.3595 0.0402  -0.0219 -0.0041 295 ARG A N   
824  C CA  . ARG A 116 ? 0.2981 0.4440 0.3431 0.0312  -0.0170 -0.0037 295 ARG A CA  
825  C C   . ARG A 116 ? 0.2851 0.4434 0.3289 0.0228  -0.0147 -0.0075 295 ARG A C   
826  O O   . ARG A 116 ? 0.2732 0.4493 0.3258 0.0232  -0.0162 -0.0110 295 ARG A O   
827  C CB  . ARG A 116 ? 0.2978 0.4330 0.3415 0.0307  -0.0117 -0.0063 295 ARG A CB  
828  C CG  . ARG A 116 ? 0.2993 0.4462 0.3511 0.0308  -0.0079 -0.0135 295 ARG A CG  
829  C CD  . ARG A 116 ? 0.3110 0.4491 0.3566 0.0259  -0.0023 -0.0155 295 ARG A CD  
830  N NE  . ARG A 116 ? 0.3041 0.4529 0.3559 0.0261  0.0017  -0.0224 295 ARG A NE  
831  C CZ  . ARG A 116 ? 0.3027 0.4674 0.3580 0.0210  0.0048  -0.0267 295 ARG A CZ  
832  N NH1 . ARG A 116 ? 0.2875 0.4625 0.3482 0.0212  0.0091  -0.0333 295 ARG A NH1 
833  N NH2 . ARG A 116 ? 0.2897 0.4604 0.3427 0.0150  0.0039  -0.0249 295 ARG A NH2 
834  N N   . THR A 117 ? 0.2790 0.4277 0.3127 0.0152  -0.0110 -0.0070 296 THR A N   
835  C CA  . THR A 117 ? 0.2704 0.4254 0.3016 0.0061  -0.0079 -0.0107 296 THR A CA  
836  C C   . THR A 117 ? 0.2715 0.4297 0.3064 0.0034  -0.0028 -0.0148 296 THR A C   
837  O O   . THR A 117 ? 0.2642 0.4186 0.3020 0.0083  -0.0015 -0.0152 296 THR A O   
838  C CB  . THR A 117 ? 0.2802 0.4212 0.3002 0.0003  -0.0056 -0.0089 296 THR A CB  
839  O OG1 . THR A 117 ? 0.2842 0.4107 0.3010 0.0016  -0.0025 -0.0071 296 THR A OG1 
840  C CG2 . THR A 117 ? 0.2811 0.4194 0.2954 0.0016  -0.0094 -0.0053 296 THR A CG2 
841  N N   . LYS A 118 ? 0.2689 0.4336 0.3025 -0.0053 0.0002  -0.0179 297 LYS A N   
842  C CA  . LYS A 118 ? 0.2786 0.4413 0.3105 -0.0107 0.0055  -0.0199 297 LYS A CA  
843  C C   . LYS A 118 ? 0.2781 0.4201 0.3003 -0.0118 0.0073  -0.0159 297 LYS A C   
844  O O   . LYS A 118 ? 0.2868 0.4184 0.3051 -0.0088 0.0051  -0.0128 297 LYS A O   
845  C CB  . LYS A 118 ? 0.2995 0.4723 0.3316 -0.0210 0.0080  -0.0231 297 LYS A CB  
846  C CG  . LYS A 118 ? 0.3091 0.5062 0.3527 -0.0209 0.0068  -0.0278 297 LYS A CG  
847  C CD  . LYS A 118 ? 0.3305 0.5371 0.3737 -0.0330 0.0096  -0.0310 297 LYS A CD  
848  C CE  . LYS A 118 ? 0.3386 0.5725 0.3951 -0.0336 0.0084  -0.0361 297 LYS A CE  
849  N NZ  . LYS A 118 ? 0.3589 0.6015 0.4200 -0.0289 0.0014  -0.0356 297 LYS A NZ  
850  N N   . ALA A 119 ? 0.2761 0.4134 0.2946 -0.0163 0.0111  -0.0159 298 ALA A N   
851  C CA  . ALA A 119 ? 0.2852 0.4047 0.2960 -0.0171 0.0119  -0.0118 298 ALA A CA  
852  C C   . ALA A 119 ? 0.2922 0.4026 0.2972 -0.0242 0.0130  -0.0105 298 ALA A C   
853  O O   . ALA A 119 ? 0.2975 0.4124 0.3015 -0.0319 0.0151  -0.0122 298 ALA A O   
854  C CB  . ALA A 119 ? 0.2762 0.3946 0.2848 -0.0184 0.0144  -0.0116 298 ALA A CB  
855  N N   . MET A 120 ? 0.3003 0.3978 0.3020 -0.0216 0.0119  -0.0079 299 MET A N   
856  C CA  . MET A 120 ? 0.3142 0.3999 0.3111 -0.0268 0.0132  -0.0072 299 MET A CA  
857  C C   . MET A 120 ? 0.3133 0.3860 0.3067 -0.0270 0.0140  -0.0029 299 MET A C   
858  O O   . MET A 120 ? 0.3128 0.3791 0.3066 -0.0214 0.0128  -0.0002 299 MET A O   
859  C CB  . MET A 120 ? 0.3324 0.4128 0.3282 -0.0239 0.0122  -0.0079 299 MET A CB  
860  C CG  . MET A 120 ? 0.3577 0.4245 0.3497 -0.0281 0.0142  -0.0086 299 MET A CG  
861  S SD  . MET A 120 ? 0.3906 0.4521 0.3811 -0.0244 0.0145  -0.0106 299 MET A SD  
862  C CE  . MET A 120 ? 0.3749 0.4279 0.3679 -0.0171 0.0143  -0.0056 299 MET A CE  
863  N N   . VAL A 121 ? 0.3128 0.3824 0.3026 -0.0341 0.0158  -0.0017 300 VAL A N   
864  C CA  . VAL A 121 ? 0.3207 0.3774 0.3062 -0.0353 0.0156  0.0036  300 VAL A CA  
865  C C   . VAL A 121 ? 0.3232 0.3642 0.3077 -0.0357 0.0155  0.0046  300 VAL A C   
866  O O   . VAL A 121 ? 0.3091 0.3474 0.2923 -0.0414 0.0171  0.0018  300 VAL A O   
867  C CB  . VAL A 121 ? 0.3251 0.3848 0.3057 -0.0435 0.0173  0.0054  300 VAL A CB  
868  C CG1 . VAL A 121 ? 0.3265 0.3728 0.3011 -0.0448 0.0159  0.0125  300 VAL A CG1 
869  C CG2 . VAL A 121 ? 0.3229 0.4004 0.3059 -0.0430 0.0185  0.0021  300 VAL A CG2 
870  N N   . ALA A 122 ? 0.3267 0.3581 0.3126 -0.0296 0.0139  0.0079  301 ALA A N   
871  C CA  . ALA A 122 ? 0.3301 0.3474 0.3172 -0.0282 0.0143  0.0078  301 ALA A CA  
872  C C   . ALA A 122 ? 0.3399 0.3435 0.3257 -0.0277 0.0123  0.0144  301 ALA A C   
873  O O   . ALA A 122 ? 0.3477 0.3537 0.3329 -0.0252 0.0099  0.0191  301 ALA A O   
874  C CB  . ALA A 122 ? 0.3256 0.3451 0.3175 -0.0210 0.0144  0.0050  301 ALA A CB  
875  N N   . CYS A 123 ? 0.3485 0.3373 0.3336 -0.0303 0.0131  0.0147  302 CYS A N   
876  C CA  . CYS A 123 ? 0.3693 0.3424 0.3540 -0.0291 0.0105  0.0217  302 CYS A CA  
877  C C   . CYS A 123 ? 0.3733 0.3334 0.3648 -0.0232 0.0112  0.0190  302 CYS A C   
878  O O   . CYS A 123 ? 0.3708 0.3252 0.3623 -0.0261 0.0144  0.0127  302 CYS A O   
879  C CB  . CYS A 123 ? 0.3884 0.3528 0.3652 -0.0390 0.0107  0.0256  302 CYS A CB  
880  S SG  . CYS A 123 ? 0.4239 0.3657 0.3990 -0.0379 0.0063  0.0361  302 CYS A SG  
881  N N   . TYR A 124 ? 0.3790 0.3361 0.3769 -0.0150 0.0083  0.0228  303 TYR A N   
882  C CA  . TYR A 124 ? 0.3994 0.3434 0.4055 -0.0084 0.0087  0.0212  303 TYR A CA  
883  C C   . TYR A 124 ? 0.4208 0.3481 0.4264 -0.0080 0.0042  0.0303  303 TYR A C   
884  O O   . TYR A 124 ? 0.4117 0.3421 0.4183 -0.0047 -0.0008 0.0380  303 TYR A O   
885  C CB  . TYR A 124 ? 0.3950 0.3489 0.4107 0.0006  0.0088  0.0188  303 TYR A CB  
886  C CG  . TYR A 124 ? 0.3948 0.3630 0.4102 0.0002  0.0129  0.0111  303 TYR A CG  
887  C CD1 . TYR A 124 ? 0.3884 0.3708 0.3989 -0.0026 0.0122  0.0119  303 TYR A CD1 
888  C CD2 . TYR A 124 ? 0.4028 0.3695 0.4223 0.0025  0.0175  0.0029  303 TYR A CD2 
889  C CE1 . TYR A 124 ? 0.3934 0.3873 0.4032 -0.0028 0.0150  0.0063  303 TYR A CE1 
890  C CE2 . TYR A 124 ? 0.4061 0.3857 0.4234 0.0014  0.0207  -0.0030 303 TYR A CE2 
891  C CZ  . TYR A 124 ? 0.4001 0.3928 0.4127 -0.0011 0.0190  -0.0005 303 TYR A CZ  
892  O OH  . TYR A 124 ? 0.4076 0.4114 0.4177 -0.0019 0.0212  -0.0049 303 TYR A OH  
893  N N   . PRO A 125 ? 0.4547 0.3633 0.4583 -0.0118 0.0053  0.0299  304 PRO A N   
894  C CA  . PRO A 125 ? 0.4915 0.3826 0.4911 -0.0141 0.0006  0.0403  304 PRO A CA  
895  C C   . PRO A 125 ? 0.5242 0.4046 0.5344 -0.0031 -0.0043 0.0459  304 PRO A C   
896  O O   . PRO A 125 ? 0.5651 0.4250 0.5749 -0.0030 -0.0077 0.0528  304 PRO A O   
897  C CB  . PRO A 125 ? 0.4904 0.3644 0.4857 -0.0219 0.0043  0.0360  304 PRO A CB  
898  C CG  . PRO A 125 ? 0.4739 0.3512 0.4766 -0.0176 0.0097  0.0231  304 PRO A CG  
899  C CD  . PRO A 125 ? 0.4661 0.3687 0.4704 -0.0146 0.0108  0.0196  304 PRO A CD  
900  N N   . GLY A 126 ? 0.5229 0.4177 0.5431 0.0059  -0.0049 0.0434  305 GLY A N   
901  C CA  . GLY A 126 ? 0.5411 0.4303 0.5750 0.0175  -0.0088 0.0466  305 GLY A CA  
902  C C   . GLY A 126 ? 0.5711 0.4441 0.6144 0.0227  -0.0047 0.0387  305 GLY A C   
903  O O   . GLY A 126 ? 0.5870 0.4593 0.6270 0.0180  0.0020  0.0285  305 GLY A O   
904  N N   . ASN A 127 ? 0.5674 0.4281 0.6228 0.0326  -0.0090 0.0431  306 ASN A N   
905  C CA  . ASN A 127 ? 0.5806 0.4232 0.6464 0.0389  -0.0055 0.0358  306 ASN A CA  
906  C C   . ASN A 127 ? 0.5431 0.3997 0.6173 0.0429  0.0029  0.0208  306 ASN A C   
907  O O   . ASN A 127 ? 0.5457 0.3919 0.6206 0.0416  0.0093  0.0102  306 ASN A O   
908  C CB  . ASN A 127 ? 0.6354 0.4534 0.6905 0.0299  -0.0041 0.0363  306 ASN A CB  
909  C CG  . ASN A 127 ? 0.6841 0.4859 0.7313 0.0263  -0.0124 0.0521  306 ASN A CG  
910  O OD1 . ASN A 127 ? 0.7017 0.5028 0.7329 0.0139  -0.0128 0.0573  306 ASN A OD1 
911  N ND2 . ASN A 127 ? 0.6953 0.4849 0.7538 0.0370  -0.0191 0.0602  306 ASN A ND2 
912  N N   . GLY A 128 ? 0.5033 0.3837 0.5830 0.0466  0.0029  0.0201  307 GLY A N   
913  C CA  . GLY A 128 ? 0.4883 0.3832 0.5776 0.0515  0.0100  0.0080  307 GLY A CA  
914  C C   . GLY A 128 ? 0.4803 0.3865 0.5573 0.0421  0.0167  -0.0005 307 GLY A C   
915  O O   . GLY A 128 ? 0.4773 0.3947 0.5589 0.0442  0.0230  -0.0105 307 GLY A O   
916  N N   . THR A 129 ? 0.4910 0.3952 0.5524 0.0317  0.0150  0.0038  308 THR A N   
917  C CA  . THR A 129 ? 0.4995 0.4139 0.5498 0.0230  0.0200  -0.0033 308 THR A CA  
918  C C   . THR A 129 ? 0.4877 0.4252 0.5381 0.0237  0.0202  -0.0029 308 THR A C   
919  O O   . THR A 129 ? 0.4803 0.4252 0.5323 0.0257  0.0150  0.0055  308 THR A O   
920  C CB  . THR A 129 ? 0.5102 0.4177 0.5464 0.0121  0.0182  0.0008  308 THR A CB  
921  O OG1 . THR A 129 ? 0.5263 0.4383 0.5589 0.0110  0.0119  0.0123  308 THR A OG1 
922  C CG2 . THR A 129 ? 0.5093 0.3927 0.5437 0.0090  0.0188  -0.0005 308 THR A CG2 
923  N N   . GLY A 130 ? 0.4738 0.4218 0.5216 0.0214  0.0260  -0.0119 309 GLY A N   
924  C CA  . GLY A 130 ? 0.4482 0.4158 0.4944 0.0209  0.0267  -0.0118 309 GLY A CA  
925  C C   . GLY A 130 ? 0.4349 0.4099 0.4710 0.0141  0.0311  -0.0189 309 GLY A C   
926  O O   . GLY A 130 ? 0.4317 0.3990 0.4600 0.0080  0.0320  -0.0221 309 GLY A O   
927  N N   . TYR A 131 ? 0.4103 0.4005 0.4465 0.0148  0.0333  -0.0209 310 TYR A N   
928  C CA  . TYR A 131 ? 0.4094 0.4080 0.4357 0.0089  0.0364  -0.0262 310 TYR A CA  
929  C C   . TYR A 131 ? 0.3909 0.4009 0.4207 0.0115  0.0411  -0.0306 310 TYR A C   
930  O O   . TYR A 131 ? 0.3733 0.3915 0.4089 0.0149  0.0398  -0.0259 310 TYR A O   
931  C CB  . TYR A 131 ? 0.4324 0.4386 0.4505 0.0043  0.0320  -0.0201 310 TYR A CB  
932  C CG  . TYR A 131 ? 0.4563 0.4678 0.4639 -0.0024 0.0330  -0.0242 310 TYR A CG  
933  C CD1 . TYR A 131 ? 0.4718 0.4926 0.4749 -0.0039 0.0362  -0.0290 310 TYR A CD1 
934  C CD2 . TYR A 131 ? 0.4938 0.5025 0.4958 -0.0078 0.0304  -0.0231 310 TYR A CD2 
935  C CE1 . TYR A 131 ? 0.4976 0.5244 0.4909 -0.0101 0.0359  -0.0320 310 TYR A CE1 
936  C CE2 . TYR A 131 ? 0.5128 0.5287 0.5068 -0.0139 0.0305  -0.0268 310 TYR A CE2 
937  C CZ  . TYR A 131 ? 0.5204 0.5453 0.5099 -0.0147 0.0327  -0.0311 310 TYR A CZ  
938  O OH  . TYR A 131 ? 0.5564 0.5895 0.5377 -0.0207 0.0316  -0.0340 310 TYR A OH  
939  N N   . VAL A 132 ? 0.3758 0.3866 0.4014 0.0089  0.0469  -0.0400 311 VAL A N   
940  C CA  . VAL A 132 ? 0.3748 0.3964 0.4025 0.0101  0.0528  -0.0454 311 VAL A CA  
941  C C   . VAL A 132 ? 0.3625 0.3977 0.3823 0.0063  0.0510  -0.0399 311 VAL A C   
942  O O   . VAL A 132 ? 0.3575 0.3934 0.3692 0.0025  0.0461  -0.0347 311 VAL A O   
943  C CB  . VAL A 132 ? 0.3915 0.4107 0.4143 0.0071  0.0597  -0.0576 311 VAL A CB  
944  C CG1 . VAL A 132 ? 0.3935 0.3973 0.4261 0.0120  0.0621  -0.0639 311 VAL A CG1 
945  C CG2 . VAL A 132 ? 0.3980 0.4184 0.4052 -0.0017 0.0583  -0.0596 311 VAL A CG2 
946  N N   . ARG A 133 ? 0.3400 0.3857 0.3629 0.0073  0.0553  -0.0414 312 ARG A N   
947  C CA  . ARG A 133 ? 0.3477 0.4046 0.3632 0.0035  0.0543  -0.0361 312 ARG A CA  
948  C C   . ARG A 133 ? 0.3412 0.3996 0.3410 -0.0033 0.0528  -0.0368 312 ARG A C   
949  O O   . ARG A 133 ? 0.3348 0.3925 0.3282 -0.0066 0.0568  -0.0450 312 ARG A O   
950  C CB  . ARG A 133 ? 0.3602 0.4279 0.3802 0.0037  0.0613  -0.0400 312 ARG A CB  
951  C CG  . ARG A 133 ? 0.3831 0.4605 0.3985 0.0002  0.0601  -0.0328 312 ARG A CG  
952  C CD  . ARG A 133 ? 0.4100 0.4989 0.4304 -0.0007 0.0681  -0.0375 312 ARG A CD  
953  N NE  . ARG A 133 ? 0.4323 0.5298 0.4457 -0.0062 0.0681  -0.0310 312 ARG A NE  
954  C CZ  . ARG A 133 ? 0.4349 0.5413 0.4574 -0.0063 0.0707  -0.0287 312 ARG A CZ  
955  N NH1 . ARG A 133 ? 0.4176 0.5274 0.4578 -0.0003 0.0731  -0.0325 312 ARG A NH1 
956  N NH2 . ARG A 133 ? 0.4515 0.5632 0.4656 -0.0127 0.0705  -0.0223 312 ARG A NH2 
957  N N   . HIS A 134 ? 0.3304 0.3911 0.3246 -0.0050 0.0468  -0.0286 313 HIS A N   
958  C CA  . HIS A 134 ? 0.3396 0.4033 0.3210 -0.0103 0.0436  -0.0276 313 HIS A CA  
959  C C   . HIS A 134 ? 0.3496 0.4179 0.3276 -0.0105 0.0383  -0.0182 313 HIS A C   
960  O O   . HIS A 134 ? 0.3326 0.3995 0.3181 -0.0071 0.0365  -0.0128 313 HIS A O   
961  C CB  . HIS A 134 ? 0.3377 0.3946 0.3186 -0.0111 0.0402  -0.0294 313 HIS A CB  
962  C CG  . HIS A 134 ? 0.3306 0.3829 0.3184 -0.0076 0.0351  -0.0226 313 HIS A CG  
963  N ND1 . HIS A 134 ? 0.3291 0.3745 0.3272 -0.0029 0.0355  -0.0215 313 HIS A ND1 
964  C CD2 . HIS A 134 ? 0.3337 0.3883 0.3194 -0.0080 0.0295  -0.0171 313 HIS A CD2 
965  C CE1 . HIS A 134 ? 0.3392 0.3827 0.3393 -0.0017 0.0305  -0.0154 313 HIS A CE1 
966  N NE2 . HIS A 134 ? 0.3233 0.3725 0.3165 -0.0046 0.0273  -0.0133 313 HIS A NE2 
967  N N   . VAL A 135 ? 0.3578 0.4312 0.3246 -0.0146 0.0354  -0.0164 314 VAL A N   
968  C CA  . VAL A 135 ? 0.3570 0.4326 0.3206 -0.0141 0.0291  -0.0077 314 VAL A CA  
969  C C   . VAL A 135 ? 0.3495 0.4252 0.3124 -0.0140 0.0236  -0.0075 314 VAL A C   
970  O O   . VAL A 135 ? 0.3411 0.4194 0.2988 -0.0176 0.0240  -0.0129 314 VAL A O   
971  C CB  . VAL A 135 ? 0.3749 0.4570 0.3270 -0.0184 0.0292  -0.0043 314 VAL A CB  
972  C CG1 . VAL A 135 ? 0.3772 0.4606 0.3249 -0.0177 0.0215  0.0043  314 VAL A CG1 
973  C CG2 . VAL A 135 ? 0.3660 0.4494 0.3199 -0.0192 0.0346  -0.0031 314 VAL A CG2 
974  N N   . ASP A 136 ? 0.3415 0.4154 0.3100 -0.0103 0.0189  -0.0020 315 ASP A N   
975  C CA  . ASP A 136 ? 0.3587 0.4347 0.3286 -0.0098 0.0143  -0.0019 315 ASP A CA  
976  C C   . ASP A 136 ? 0.3678 0.4526 0.3297 -0.0125 0.0102  -0.0008 315 ASP A C   
977  O O   . ASP A 136 ? 0.3755 0.4650 0.3355 -0.0157 0.0091  -0.0052 315 ASP A O   
978  C CB  . ASP A 136 ? 0.3426 0.4162 0.3198 -0.0052 0.0109  0.0029  315 ASP A CB  
979  C CG  . ASP A 136 ? 0.3378 0.4048 0.3224 -0.0035 0.0131  0.0014  315 ASP A CG  
980  O OD1 . ASP A 136 ? 0.3345 0.3977 0.3199 -0.0050 0.0169  -0.0029 315 ASP A OD1 
981  O OD2 . ASP A 136 ? 0.3272 0.3925 0.3164 -0.0005 0.0108  0.0044  315 ASP A OD2 
982  N N   . ASN A 137 ? 0.3624 0.4492 0.3196 -0.0116 0.0074  0.0056  316 ASN A N   
983  C CA  . ASN A 137 ? 0.3785 0.4734 0.3278 -0.0133 0.0019  0.0088  316 ASN A CA  
984  C C   . ASN A 137 ? 0.3885 0.4848 0.3262 -0.0175 0.0040  0.0111  316 ASN A C   
985  O O   . ASN A 137 ? 0.3820 0.4754 0.3171 -0.0162 0.0020  0.0188  316 ASN A O   
986  C CB  . ASN A 137 ? 0.3754 0.4712 0.3301 -0.0076 -0.0050 0.0158  316 ASN A CB  
987  C CG  . ASN A 137 ? 0.3834 0.4875 0.3313 -0.0080 -0.0120 0.0209  316 ASN A CG  
988  O OD1 . ASN A 137 ? 0.3851 0.4968 0.3240 -0.0133 -0.0125 0.0183  316 ASN A OD1 
989  N ND2 . ASN A 137 ? 0.3778 0.4801 0.3298 -0.0022 -0.0179 0.0280  316 ASN A ND2 
990  N N   . PRO A 138 ? 0.4010 0.5011 0.3308 -0.0234 0.0085  0.0042  317 PRO A N   
991  C CA  . PRO A 138 ? 0.4286 0.5322 0.3455 -0.0286 0.0111  0.0054  317 PRO A CA  
992  C C   . PRO A 138 ? 0.4491 0.5619 0.3530 -0.0325 0.0045  0.0099  317 PRO A C   
993  O O   . PRO A 138 ? 0.4472 0.5627 0.3389 -0.0369 0.0052  0.0141  317 PRO A O   
994  C CB  . PRO A 138 ? 0.4207 0.5241 0.3364 -0.0326 0.0195  -0.0061 317 PRO A CB  
995  C CG  . PRO A 138 ? 0.4155 0.5186 0.3372 -0.0321 0.0176  -0.0122 317 PRO A CG  
996  C CD  . PRO A 138 ? 0.4106 0.5107 0.3432 -0.0258 0.0120  -0.0057 317 PRO A CD  
997  N N   . ASN A 139 ? 0.4715 0.5904 0.3781 -0.0314 -0.0021 0.0093  318 ASN A N   
998  C CA  . ASN A 139 ? 0.4936 0.6238 0.3887 -0.0355 -0.0089 0.0120  318 ASN A CA  
999  C C   . ASN A 139 ? 0.4864 0.6197 0.3868 -0.0292 -0.0193 0.0223  318 ASN A C   
1000 O O   . ASN A 139 ? 0.4781 0.6226 0.3742 -0.0306 -0.0269 0.0243  318 ASN A O   
1001 C CB  . ASN A 139 ? 0.5201 0.6584 0.4127 -0.0412 -0.0080 0.0014  318 ASN A CB  
1002 C CG  . ASN A 139 ? 0.5495 0.6837 0.4371 -0.0469 0.0021  -0.0097 318 ASN A CG  
1003 O OD1 . ASN A 139 ? 0.5794 0.7081 0.4755 -0.0466 0.0068  -0.0181 318 ASN A OD1 
1004 N ND2 . ASN A 139 ? 0.5454 0.6818 0.4191 -0.0521 0.0058  -0.0097 318 ASN A ND2 
1005 N N   . GLY A 140 ? 0.4719 0.5953 0.3819 -0.0222 -0.0197 0.0283  319 GLY A N   
1006 C CA  . GLY A 140 ? 0.4536 0.5768 0.3697 -0.0150 -0.0287 0.0377  319 GLY A CA  
1007 C C   . GLY A 140 ? 0.4306 0.5648 0.3569 -0.0114 -0.0347 0.0347  319 GLY A C   
1008 O O   . GLY A 140 ? 0.4075 0.5514 0.3318 -0.0099 -0.0435 0.0401  319 GLY A O   
1009 N N   . ASP A 141 ? 0.4209 0.5543 0.3588 -0.0099 -0.0301 0.0267  320 ASP A N   
1010 C CA  . ASP A 141 ? 0.4090 0.5543 0.3570 -0.0082 -0.0341 0.0226  320 ASP A CA  
1011 C C   . ASP A 141 ? 0.3855 0.5295 0.3480 0.0015  -0.0380 0.0265  320 ASP A C   
1012 O O   . ASP A 141 ? 0.3859 0.5406 0.3592 0.0039  -0.0405 0.0229  320 ASP A O   
1013 C CB  . ASP A 141 ? 0.4247 0.5710 0.3752 -0.0139 -0.0273 0.0118  320 ASP A CB  
1014 C CG  . ASP A 141 ? 0.4498 0.5835 0.4083 -0.0113 -0.0203 0.0089  320 ASP A CG  
1015 O OD1 . ASP A 141 ? 0.4394 0.5638 0.4007 -0.0059 -0.0199 0.0142  320 ASP A OD1 
1016 O OD2 . ASP A 141 ? 0.4725 0.6057 0.4340 -0.0152 -0.0157 0.0015  320 ASP A OD2 
1017 N N   . GLY A 142 ? 0.3677 0.4987 0.3305 0.0065  -0.0379 0.0332  321 GLY A N   
1018 C CA  . GLY A 142 ? 0.3498 0.4778 0.3252 0.0159  -0.0417 0.0365  321 GLY A CA  
1019 C C   . GLY A 142 ? 0.3416 0.4571 0.3237 0.0182  -0.0351 0.0333  321 GLY A C   
1020 O O   . GLY A 142 ? 0.3439 0.4519 0.3330 0.0250  -0.0372 0.0365  321 GLY A O   
1021 N N   . ARG A 143 ? 0.3288 0.4417 0.3086 0.0124  -0.0276 0.0268  322 ARG A N   
1022 C CA  . ARG A 143 ? 0.3306 0.4338 0.3162 0.0138  -0.0220 0.0237  322 ARG A CA  
1023 C C   . ARG A 143 ? 0.3331 0.4227 0.3137 0.0139  -0.0201 0.0289  322 ARG A C   
1024 O O   . ARG A 143 ? 0.3300 0.4173 0.3013 0.0086  -0.0173 0.0301  322 ARG A O   
1025 C CB  . ARG A 143 ? 0.3281 0.4327 0.3130 0.0080  -0.0158 0.0164  322 ARG A CB  
1026 C CG  . ARG A 143 ? 0.3345 0.4516 0.3249 0.0065  -0.0168 0.0110  322 ARG A CG  
1027 C CD  . ARG A 143 ? 0.3404 0.4564 0.3290 -0.0001 -0.0112 0.0045  322 ARG A CD  
1028 N NE  . ARG A 143 ? 0.3518 0.4670 0.3306 -0.0061 -0.0094 0.0027  322 ARG A NE  
1029 C CZ  . ARG A 143 ? 0.3578 0.4635 0.3325 -0.0093 -0.0036 -0.0001 322 ARG A CZ  
1030 N NH1 . ARG A 143 ? 0.3660 0.4625 0.3456 -0.0074 0.0000  -0.0004 322 ARG A NH1 
1031 N NH2 . ARG A 143 ? 0.3646 0.4708 0.3306 -0.0144 -0.0017 -0.0031 322 ARG A NH2 
1032 N N   . CYS A 144 ? 0.3273 0.4085 0.3143 0.0192  -0.0212 0.0312  323 CYS A N   
1033 C CA  . CYS A 144 ? 0.3347 0.4031 0.3177 0.0187  -0.0202 0.0366  323 CYS A CA  
1034 C C   . CYS A 144 ? 0.3247 0.3859 0.3122 0.0178  -0.0148 0.0327  323 CYS A C   
1035 O O   . CYS A 144 ? 0.3271 0.3816 0.3107 0.0142  -0.0117 0.0349  323 CYS A O   
1036 C CB  . CYS A 144 ? 0.3564 0.4182 0.3409 0.0243  -0.0267 0.0438  323 CYS A CB  
1037 S SG  . CYS A 144 ? 0.3999 0.4609 0.3991 0.0336  -0.0294 0.0400  323 CYS A SG  
1038 N N   . VAL A 145 ? 0.3054 0.3693 0.3010 0.0205  -0.0138 0.0272  324 VAL A N   
1039 C CA  . VAL A 145 ? 0.3037 0.3617 0.3027 0.0195  -0.0098 0.0240  324 VAL A CA  
1040 C C   . VAL A 145 ? 0.3023 0.3671 0.3033 0.0171  -0.0065 0.0181  324 VAL A C   
1041 O O   . VAL A 145 ? 0.2985 0.3711 0.3031 0.0186  -0.0076 0.0149  324 VAL A O   
1042 C CB  . VAL A 145 ? 0.3108 0.3620 0.3158 0.0242  -0.0117 0.0236  324 VAL A CB  
1043 C CG1 . VAL A 145 ? 0.3099 0.3573 0.3173 0.0222  -0.0081 0.0198  324 VAL A CG1 
1044 C CG2 . VAL A 145 ? 0.3038 0.3446 0.3065 0.0258  -0.0149 0.0301  324 VAL A CG2 
1045 N N   . THR A 146 ? 0.2945 0.3560 0.2937 0.0134  -0.0026 0.0170  325 THR A N   
1046 C CA  . THR A 146 ? 0.2877 0.3516 0.2886 0.0112  0.0002  0.0128  325 THR A CA  
1047 C C   . THR A 146 ? 0.2951 0.3552 0.2999 0.0124  0.0006  0.0118  325 THR A C   
1048 O O   . THR A 146 ? 0.3001 0.3542 0.3055 0.0126  0.0006  0.0137  325 THR A O   
1049 C CB  . THR A 146 ? 0.2875 0.3495 0.2856 0.0077  0.0037  0.0122  325 THR A CB  
1050 O OG1 . THR A 146 ? 0.2780 0.3437 0.2708 0.0058  0.0038  0.0123  325 THR A OG1 
1051 C CG2 . THR A 146 ? 0.2821 0.3437 0.2819 0.0058  0.0060  0.0090  325 THR A CG2 
1052 N N   . CYS A 147 ? 0.2914 0.3558 0.2981 0.0121  0.0010  0.0085  326 CYS A N   
1053 C CA  . CYS A 147 ? 0.3027 0.3650 0.3111 0.0121  0.0015  0.0069  326 CYS A CA  
1054 C C   . CYS A 147 ? 0.2990 0.3627 0.3056 0.0082  0.0035  0.0058  326 CYS A C   
1055 O O   . CYS A 147 ? 0.2810 0.3505 0.2872 0.0063  0.0043  0.0037  326 CYS A O   
1056 C CB  . CYS A 147 ? 0.3199 0.3864 0.3317 0.0155  0.0003  0.0039  326 CYS A CB  
1057 S SG  . CYS A 147 ? 0.3444 0.4093 0.3565 0.0147  0.0014  0.0005  326 CYS A SG  
1058 N N   . ILE A 148 ? 0.2982 0.3567 0.3042 0.0068  0.0038  0.0076  327 ILE A N   
1059 C CA  . ILE A 148 ? 0.3013 0.3584 0.3054 0.0036  0.0047  0.0082  327 ILE A CA  
1060 C C   . ILE A 148 ? 0.3003 0.3568 0.3030 0.0024  0.0036  0.0087  327 ILE A C   
1061 O O   . ILE A 148 ? 0.3135 0.3682 0.3176 0.0037  0.0022  0.0093  327 ILE A O   
1062 C CB  . ILE A 148 ? 0.2936 0.3456 0.2989 0.0036  0.0055  0.0103  327 ILE A CB  
1063 C CG1 . ILE A 148 ? 0.2984 0.3514 0.3035 0.0042  0.0069  0.0092  327 ILE A CG1 
1064 C CG2 . ILE A 148 ? 0.3004 0.3486 0.3043 0.0010  0.0059  0.0115  327 ILE A CG2 
1065 C CD1 . ILE A 148 ? 0.2906 0.3398 0.2975 0.0045  0.0088  0.0096  327 ILE A CD1 
1066 N N   . TYR A 149 ? 0.2869 0.3452 0.2859 -0.0012 0.0043  0.0085  328 TYR A N   
1067 C CA  . TYR A 149 ? 0.2897 0.3480 0.2848 -0.0038 0.0032  0.0096  328 TYR A CA  
1068 C C   . TYR A 149 ? 0.2931 0.3460 0.2854 -0.0067 0.0022  0.0145  328 TYR A C   
1069 O O   . TYR A 149 ? 0.2836 0.3347 0.2746 -0.0091 0.0037  0.0150  328 TYR A O   
1070 C CB  . TYR A 149 ? 0.2897 0.3557 0.2817 -0.0063 0.0051  0.0055  328 TYR A CB  
1071 C CG  . TYR A 149 ? 0.2940 0.3615 0.2796 -0.0102 0.0045  0.0059  328 TYR A CG  
1072 C CD1 . TYR A 149 ? 0.2924 0.3597 0.2776 -0.0090 0.0028  0.0041  328 TYR A CD1 
1073 C CD2 . TYR A 149 ? 0.2866 0.3556 0.2655 -0.0162 0.0055  0.0081  328 TYR A CD2 
1074 C CE1 . TYR A 149 ? 0.2872 0.3570 0.2650 -0.0134 0.0020  0.0040  328 TYR A CE1 
1075 C CE2 . TYR A 149 ? 0.2982 0.3693 0.2691 -0.0207 0.0048  0.0091  328 TYR A CE2 
1076 C CZ  . TYR A 149 ? 0.3043 0.3765 0.2744 -0.0192 0.0029  0.0067  328 TYR A CZ  
1077 O OH  . TYR A 149 ? 0.2985 0.3738 0.2593 -0.0245 0.0019  0.0071  328 TYR A OH  
1078 N N   . TYR A 150 ? 0.2979 0.3479 0.2897 -0.0065 -0.0009 0.0181  329 TYR A N   
1079 C CA  . TYR A 150 ? 0.3027 0.3467 0.2929 -0.0080 -0.0032 0.0237  329 TYR A CA  
1080 C C   . TYR A 150 ? 0.3215 0.3672 0.3030 -0.0131 -0.0051 0.0265  329 TYR A C   
1081 O O   . TYR A 150 ? 0.3097 0.3614 0.2879 -0.0144 -0.0056 0.0239  329 TYR A O   
1082 C CB  . TYR A 150 ? 0.2990 0.3403 0.2965 -0.0036 -0.0059 0.0265  329 TYR A CB  
1083 C CG  . TYR A 150 ? 0.2980 0.3384 0.3028 0.0004  -0.0033 0.0238  329 TYR A CG  
1084 C CD1 . TYR A 150 ? 0.2889 0.3241 0.2955 0.0011  -0.0010 0.0234  329 TYR A CD1 
1085 C CD2 . TYR A 150 ? 0.2942 0.3386 0.3030 0.0025  -0.0029 0.0214  329 TYR A CD2 
1086 C CE1 . TYR A 150 ? 0.2921 0.3276 0.3036 0.0039  0.0017  0.0203  329 TYR A CE1 
1087 C CE2 . TYR A 150 ? 0.2933 0.3376 0.3069 0.0050  -0.0003 0.0195  329 TYR A CE2 
1088 C CZ  . TYR A 150 ? 0.2949 0.3356 0.3095 0.0057  0.0021  0.0187  329 TYR A CZ  
1089 O OH  . TYR A 150 ? 0.3004 0.3421 0.3181 0.0073  0.0051  0.0163  329 TYR A OH  
1090 N N   . LEU A 151 ? 0.3390 0.3786 0.3159 -0.0164 -0.0062 0.0319  330 LEU A N   
1091 C CA  . LEU A 151 ? 0.3666 0.4078 0.3328 -0.0227 -0.0077 0.0355  330 LEU A CA  
1092 C C   . LEU A 151 ? 0.3781 0.4097 0.3415 -0.0237 -0.0126 0.0449  330 LEU A C   
1093 O O   . LEU A 151 ? 0.3904 0.4188 0.3439 -0.0301 -0.0131 0.0497  330 LEU A O   
1094 C CB  . LEU A 151 ? 0.3807 0.4274 0.3408 -0.0287 -0.0026 0.0315  330 LEU A CB  
1095 C CG  . LEU A 151 ? 0.3992 0.4421 0.3617 -0.0302 0.0009  0.0304  330 LEU A CG  
1096 C CD1 . LEU A 151 ? 0.4042 0.4464 0.3770 -0.0238 0.0022  0.0259  330 LEU A CD1 
1097 C CD2 . LEU A 151 ? 0.4218 0.4523 0.3798 -0.0341 -0.0010 0.0381  330 LEU A CD2 
1098 N N   . ASN A 152 ? 0.3690 0.3965 0.3413 -0.0173 -0.0164 0.0477  331 ASN A N   
1099 C CA  . ASN A 152 ? 0.3836 0.4014 0.3568 -0.0157 -0.0217 0.0565  331 ASN A CA  
1100 C C   . ASN A 152 ? 0.3969 0.4198 0.3664 -0.0165 -0.0286 0.0620  331 ASN A C   
1101 O O   . ASN A 152 ? 0.3940 0.4229 0.3720 -0.0118 -0.0314 0.0607  331 ASN A O   
1102 C CB  . ASN A 152 ? 0.3526 0.3639 0.3394 -0.0080 -0.0213 0.0556  331 ASN A CB  
1103 C CG  . ASN A 152 ? 0.3495 0.3571 0.3382 -0.0083 -0.0148 0.0493  331 ASN A CG  
1104 O OD1 . ASN A 152 ? 0.3296 0.3291 0.3128 -0.0128 -0.0131 0.0509  331 ASN A OD1 
1105 N ND2 . ASN A 152 ? 0.3381 0.3520 0.3339 -0.0046 -0.0114 0.0424  331 ASN A ND2 
1106 N N   . LYS A 153 ? 0.4343 0.4556 0.3905 -0.0233 -0.0314 0.0684  332 LYS A N   
1107 C CA  . LYS A 153 ? 0.4686 0.4952 0.4180 -0.0257 -0.0385 0.0743  332 LYS A CA  
1108 C C   . LYS A 153 ? 0.4702 0.4928 0.4307 -0.0183 -0.0462 0.0815  332 LYS A C   
1109 O O   . LYS A 153 ? 0.4835 0.4939 0.4486 -0.0147 -0.0480 0.0875  332 LYS A O   
1110 C CB  . LYS A 153 ? 0.5056 0.5299 0.4372 -0.0353 -0.0398 0.0810  332 LYS A CB  
1111 C CG  . LYS A 153 ? 0.5415 0.5781 0.4603 -0.0433 -0.0357 0.0745  332 LYS A CG  
1112 C CD  . LYS A 153 ? 0.5773 0.6243 0.4929 -0.0440 -0.0412 0.0739  332 LYS A CD  
1113 C CE  . LYS A 153 ? 0.6043 0.6630 0.5078 -0.0515 -0.0365 0.0656  332 LYS A CE  
1114 N NZ  . LYS A 153 ? 0.6025 0.6705 0.5037 -0.0523 -0.0416 0.0632  332 LYS A NZ  
1115 N N   . ASP A 154 ? 0.4816 0.5151 0.4471 -0.0160 -0.0507 0.0802  333 ASP A N   
1116 C CA  . ASP A 154 ? 0.4847 0.5196 0.4616 -0.0094 -0.0589 0.0866  333 ASP A CA  
1117 C C   . ASP A 154 ? 0.4763 0.5031 0.4702 -0.0002 -0.0566 0.0858  333 ASP A C   
1118 O O   . ASP A 154 ? 0.4723 0.4911 0.4724 0.0049  -0.0621 0.0938  333 ASP A O   
1119 C CB  . ASP A 154 ? 0.5161 0.5483 0.4827 -0.0127 -0.0683 0.0990  333 ASP A CB  
1120 C CG  . ASP A 154 ? 0.5404 0.5821 0.4885 -0.0228 -0.0702 0.0990  333 ASP A CG  
1121 O OD1 . ASP A 154 ? 0.5558 0.6103 0.5057 -0.0239 -0.0708 0.0925  333 ASP A OD1 
1122 O OD2 . ASP A 154 ? 0.5621 0.5981 0.4937 -0.0300 -0.0708 0.1052  333 ASP A OD2 
1123 N N   . TRP A 155 ? 0.4610 0.4896 0.4620 0.0019  -0.0486 0.0760  334 TRP A N   
1124 C CA  . TRP A 155 ? 0.4390 0.4622 0.4552 0.0099  -0.0454 0.0734  334 TRP A CA  
1125 C C   . TRP A 155 ? 0.4492 0.4822 0.4816 0.0167  -0.0499 0.0739  334 TRP A C   
1126 O O   . TRP A 155 ? 0.4525 0.4983 0.4865 0.0148  -0.0508 0.0706  334 TRP A O   
1127 C CB  . TRP A 155 ? 0.3997 0.4233 0.4168 0.0091  -0.0360 0.0634  334 TRP A CB  
1128 C CG  . TRP A 155 ? 0.3666 0.3841 0.3961 0.0157  -0.0319 0.0600  334 TRP A CG  
1129 C CD1 . TRP A 155 ? 0.3538 0.3783 0.3975 0.0215  -0.0299 0.0554  334 TRP A CD1 
1130 C CD2 . TRP A 155 ? 0.3622 0.3656 0.3904 0.0163  -0.0287 0.0600  334 TRP A CD2 
1131 N NE1 . TRP A 155 ? 0.3489 0.3653 0.3998 0.0261  -0.0254 0.0521  334 TRP A NE1 
1132 C CE2 . TRP A 155 ? 0.3481 0.3507 0.3898 0.0230  -0.0248 0.0546  334 TRP A CE2 
1133 C CE3 . TRP A 155 ? 0.3661 0.3576 0.3827 0.0109  -0.0285 0.0638  334 TRP A CE3 
1134 C CZ2 . TRP A 155 ? 0.3507 0.3403 0.3945 0.0248  -0.0208 0.0520  334 TRP A CZ2 
1135 C CZ3 . TRP A 155 ? 0.3719 0.3500 0.3910 0.0122  -0.0249 0.0619  334 TRP A CZ3 
1136 C CH2 . TRP A 155 ? 0.3680 0.3448 0.4004 0.0193  -0.0212 0.0557  334 TRP A CH2 
1137 N N   . ASP A 156 ? 0.4757 0.5026 0.5210 0.0247  -0.0524 0.0777  335 ASP A N   
1138 C CA  . ASP A 156 ? 0.4870 0.5246 0.5511 0.0323  -0.0558 0.0774  335 ASP A CA  
1139 C C   . ASP A 156 ? 0.4786 0.5114 0.5572 0.0397  -0.0490 0.0712  335 ASP A C   
1140 O O   . ASP A 156 ? 0.4681 0.4877 0.5511 0.0450  -0.0497 0.0742  335 ASP A O   
1141 C CB  . ASP A 156 ? 0.5102 0.5493 0.5781 0.0357  -0.0673 0.0883  335 ASP A CB  
1142 C CG  . ASP A 156 ? 0.5133 0.5649 0.6039 0.0448  -0.0713 0.0882  335 ASP A CG  
1143 O OD1 . ASP A 156 ? 0.5091 0.5758 0.6078 0.0440  -0.0678 0.0810  335 ASP A OD1 
1144 O OD2 . ASP A 156 ? 0.5265 0.5729 0.6271 0.0526  -0.0779 0.0955  335 ASP A OD2 
1145 N N   . ALA A 157 ? 0.4721 0.5152 0.5572 0.0396  -0.0423 0.0623  336 ALA A N   
1146 C CA  . ALA A 157 ? 0.4673 0.5081 0.5626 0.0444  -0.0342 0.0547  336 ALA A CA  
1147 C C   . ALA A 157 ? 0.4716 0.5163 0.5878 0.0546  -0.0365 0.0554  336 ALA A C   
1148 O O   . ALA A 157 ? 0.4594 0.4982 0.5842 0.0600  -0.0307 0.0499  336 ALA A O   
1149 C CB  . ALA A 157 ? 0.4487 0.5000 0.5430 0.0403  -0.0274 0.0468  336 ALA A CB  
1150 N N   . LYS A 158 ? 0.4825 0.5382 0.6074 0.0573  -0.0451 0.0615  337 LYS A N   
1151 C CA  . LYS A 158 ? 0.4856 0.5473 0.6325 0.0680  -0.0490 0.0631  337 LYS A CA  
1152 C C   . LYS A 158 ? 0.4738 0.5155 0.6225 0.0748  -0.0510 0.0674  337 LYS A C   
1153 O O   . LYS A 158 ? 0.4734 0.5140 0.6403 0.0847  -0.0491 0.0641  337 LYS A O   
1154 C CB  . LYS A 158 ? 0.5041 0.5815 0.6576 0.0684  -0.0598 0.0704  337 LYS A CB  
1155 C CG  . LYS A 158 ? 0.5238 0.6235 0.6852 0.0646  -0.0579 0.0649  337 LYS A CG  
1156 C CD  . LYS A 158 ? 0.5347 0.6506 0.7228 0.0733  -0.0561 0.0604  337 LYS A CD  
1157 C CE  . LYS A 158 ? 0.5490 0.6593 0.7451 0.0783  -0.0446 0.0511  337 LYS A CE  
1158 N NZ  . LYS A 158 ? 0.5600 0.6689 0.7423 0.0693  -0.0345 0.0436  337 LYS A NZ  
1159 N N   . VAL A 159 ? 0.4717 0.4973 0.6014 0.0690  -0.0544 0.0743  338 VAL A N   
1160 C CA  . VAL A 159 ? 0.4579 0.4620 0.5863 0.0734  -0.0577 0.0806  338 VAL A CA  
1161 C C   . VAL A 159 ? 0.4470 0.4341 0.5630 0.0683  -0.0485 0.0744  338 VAL A C   
1162 O O   . VAL A 159 ? 0.4504 0.4217 0.5728 0.0739  -0.0458 0.0723  338 VAL A O   
1163 C CB  . VAL A 159 ? 0.4753 0.4740 0.5918 0.0700  -0.0693 0.0947  338 VAL A CB  
1164 C CG1 . VAL A 159 ? 0.4916 0.4646 0.6020 0.0717  -0.0723 0.1023  338 VAL A CG1 
1165 C CG2 . VAL A 159 ? 0.4742 0.4896 0.6050 0.0761  -0.0798 0.1012  338 VAL A CG2 
1166 N N   . SER A 160 ? 0.4179 0.4088 0.5171 0.0579  -0.0438 0.0709  339 SER A N   
1167 C CA  . SER A 160 ? 0.3990 0.3758 0.4844 0.0514  -0.0370 0.0668  339 SER A CA  
1168 C C   . SER A 160 ? 0.3816 0.3646 0.4704 0.0509  -0.0267 0.0542  339 SER A C   
1169 O O   . SER A 160 ? 0.3818 0.3538 0.4632 0.0473  -0.0207 0.0492  339 SER A O   
1170 C CB  . SER A 160 ? 0.4041 0.3804 0.4690 0.0405  -0.0389 0.0716  339 SER A CB  
1171 O OG  . SER A 160 ? 0.3984 0.3683 0.4575 0.0397  -0.0483 0.0838  339 SER A OG  
1172 N N   . GLY A 161 ? 0.3408 0.3416 0.4400 0.0537  -0.0248 0.0495  340 GLY A N   
1173 C CA  . GLY A 161 ? 0.3325 0.3410 0.4337 0.0524  -0.0156 0.0389  340 GLY A CA  
1174 C C   . GLY A 161 ? 0.3132 0.3223 0.3969 0.0428  -0.0119 0.0365  340 GLY A C   
1175 O O   . GLY A 161 ? 0.3200 0.3343 0.3947 0.0376  -0.0159 0.0410  340 GLY A O   
1176 N N   . GLY A 162 ? 0.3124 0.3167 0.3918 0.0406  -0.0045 0.0289  341 GLY A N   
1177 C CA  . GLY A 162 ? 0.3072 0.3111 0.3715 0.0325  -0.0015 0.0267  341 GLY A CA  
1178 C C   . GLY A 162 ? 0.2977 0.3162 0.3599 0.0295  0.0001  0.0244  341 GLY A C   
1179 O O   . GLY A 162 ? 0.3026 0.3226 0.3536 0.0238  0.0004  0.0244  341 GLY A O   
1180 N N   . ILE A 163 ? 0.2868 0.3160 0.3604 0.0334  0.0014  0.0223  342 ILE A N   
1181 C CA  . ILE A 163 ? 0.2893 0.3306 0.3615 0.0301  0.0030  0.0205  342 ILE A CA  
1182 C C   . ILE A 163 ? 0.2807 0.3215 0.3450 0.0265  0.0095  0.0147  342 ILE A C   
1183 O O   . ILE A 163 ? 0.2753 0.3127 0.3417 0.0282  0.0143  0.0095  342 ILE A O   
1184 C CB  . ILE A 163 ? 0.2948 0.3483 0.3820 0.0341  0.0031  0.0198  342 ILE A CB  
1185 C CG1 . ILE A 163 ? 0.3050 0.3623 0.3984 0.0363  -0.0050 0.0265  342 ILE A CG1 
1186 C CG2 . ILE A 163 ? 0.2935 0.3574 0.3791 0.0298  0.0069  0.0169  342 ILE A CG2 
1187 C CD1 . ILE A 163 ? 0.3161 0.3872 0.4270 0.0407  -0.0057 0.0259  342 ILE A CD1 
1188 N N   . LEU A 164 ? 0.2769 0.3207 0.3318 0.0216  0.0090  0.0154  343 LEU A N   
1189 C CA  . LEU A 164 ? 0.2726 0.3189 0.3215 0.0186  0.0138  0.0112  343 LEU A CA  
1190 C C   . LEU A 164 ? 0.2648 0.3210 0.3200 0.0186  0.0164  0.0102  343 LEU A C   
1191 O O   . LEU A 164 ? 0.2637 0.3248 0.3208 0.0173  0.0135  0.0132  343 LEU A O   
1192 C CB  . LEU A 164 ? 0.2764 0.3213 0.3142 0.0145  0.0119  0.0128  343 LEU A CB  
1193 C CG  . LEU A 164 ? 0.2854 0.3338 0.3171 0.0118  0.0149  0.0105  343 LEU A CG  
1194 C CD1 . LEU A 164 ? 0.2962 0.3425 0.3245 0.0111  0.0191  0.0059  343 LEU A CD1 
1195 C CD2 . LEU A 164 ? 0.2937 0.3416 0.3179 0.0095  0.0120  0.0122  343 LEU A CD2 
1196 N N   . ARG A 165 ? 0.2652 0.3244 0.3233 0.0194  0.0222  0.0053  344 ARG A N   
1197 C CA  . ARG A 165 ? 0.2530 0.3226 0.3161 0.0180  0.0260  0.0039  344 ARG A CA  
1198 C C   . ARG A 165 ? 0.2520 0.3221 0.3031 0.0129  0.0292  0.0027  344 ARG A C   
1199 O O   . ARG A 165 ? 0.2558 0.3224 0.3002 0.0122  0.0321  -0.0010 344 ARG A O   
1200 C CB  . ARG A 165 ? 0.2514 0.3265 0.3271 0.0223  0.0308  -0.0011 344 ARG A CB  
1201 C CG  . ARG A 165 ? 0.2516 0.3401 0.3335 0.0201  0.0358  -0.0031 344 ARG A CG  
1202 C CD  . ARG A 165 ? 0.2548 0.3515 0.3538 0.0258  0.0395  -0.0078 344 ARG A CD  
1203 N NE  . ARG A 165 ? 0.2682 0.3676 0.3798 0.0304  0.0330  -0.0035 344 ARG A NE  
1204 C CZ  . ARG A 165 ? 0.2686 0.3725 0.3970 0.0378  0.0329  -0.0057 344 ARG A CZ  
1205 N NH1 . ARG A 165 ? 0.2804 0.3848 0.4150 0.0419  0.0397  -0.0133 344 ARG A NH1 
1206 N NH2 . ARG A 165 ? 0.2611 0.3687 0.3999 0.0413  0.0257  -0.0005 344 ARG A NH2 
1207 N N   . ILE A 166 ? 0.2537 0.3275 0.3019 0.0092  0.0281  0.0063  345 ILE A N   
1208 C CA  . ILE A 166 ? 0.2594 0.3328 0.2962 0.0046  0.0299  0.0072  345 ILE A CA  
1209 C C   . ILE A 166 ? 0.2649 0.3474 0.3045 0.0010  0.0350  0.0067  345 ILE A C   
1210 O O   . ILE A 166 ? 0.2626 0.3505 0.3109 0.0003  0.0345  0.0084  345 ILE A O   
1211 C CB  . ILE A 166 ? 0.2591 0.3269 0.2891 0.0029  0.0244  0.0121  345 ILE A CB  
1212 C CG1 . ILE A 166 ? 0.2633 0.3250 0.2924 0.0058  0.0199  0.0123  345 ILE A CG1 
1213 C CG2 . ILE A 166 ? 0.2576 0.3239 0.2761 -0.0005 0.0250  0.0138  345 ILE A CG2 
1214 C CD1 . ILE A 166 ? 0.2751 0.3326 0.2992 0.0049  0.0153  0.0155  345 ILE A CD1 
1215 N N   . PHE A 167 ? 0.2794 0.3643 0.3108 -0.0021 0.0398  0.0043  346 PHE A N   
1216 C CA  . PHE A 167 ? 0.2931 0.3872 0.3243 -0.0070 0.0457  0.0038  346 PHE A CA  
1217 C C   . PHE A 167 ? 0.2946 0.3852 0.3111 -0.0129 0.0443  0.0094  346 PHE A C   
1218 O O   . PHE A 167 ? 0.2878 0.3794 0.2933 -0.0157 0.0469  0.0081  346 PHE A O   
1219 C CB  . PHE A 167 ? 0.3040 0.4048 0.3365 -0.0065 0.0533  -0.0042 346 PHE A CB  
1220 C CG  . PHE A 167 ? 0.3212 0.4218 0.3669 0.0007  0.0543  -0.0102 346 PHE A CG  
1221 C CD1 . PHE A 167 ? 0.3349 0.4254 0.3773 0.0044  0.0515  -0.0124 346 PHE A CD1 
1222 C CD2 . PHE A 167 ? 0.3204 0.4307 0.3823 0.0038  0.0578  -0.0134 346 PHE A CD2 
1223 C CE1 . PHE A 167 ? 0.3395 0.4271 0.3934 0.0108  0.0521  -0.0170 346 PHE A CE1 
1224 C CE2 . PHE A 167 ? 0.3113 0.4201 0.3861 0.0115  0.0579  -0.0182 346 PHE A CE2 
1225 C CZ  . PHE A 167 ? 0.3109 0.4070 0.3810 0.0149  0.0550  -0.0196 346 PHE A CZ  
1226 N N   . PRO A 168 ? 0.3012 0.3872 0.3169 -0.0151 0.0398  0.0160  347 PRO A N   
1227 C CA  . PRO A 168 ? 0.3103 0.3906 0.3129 -0.0199 0.0375  0.0224  347 PRO A CA  
1228 C C   . PRO A 168 ? 0.3080 0.3958 0.3030 -0.0268 0.0439  0.0229  347 PRO A C   
1229 O O   . PRO A 168 ? 0.2876 0.3850 0.2899 -0.0299 0.0497  0.0205  347 PRO A O   
1230 C CB  . PRO A 168 ? 0.3187 0.3927 0.3252 -0.0211 0.0330  0.0276  347 PRO A CB  
1231 C CG  . PRO A 168 ? 0.3069 0.3875 0.3284 -0.0190 0.0340  0.0238  347 PRO A CG  
1232 C CD  . PRO A 168 ? 0.2951 0.3803 0.3219 -0.0133 0.0361  0.0175  347 PRO A CD  
1233 N N   . GLU A 169 ? 0.3189 0.4036 0.2992 -0.0293 0.0427  0.0260  348 GLU A N   
1234 C CA  . GLU A 169 ? 0.3300 0.4219 0.2991 -0.0365 0.0484  0.0264  348 GLU A CA  
1235 C C   . GLU A 169 ? 0.3186 0.4116 0.2865 -0.0441 0.0506  0.0328  348 GLU A C   
1236 O O   . GLU A 169 ? 0.3177 0.4001 0.2827 -0.0453 0.0448  0.0408  348 GLU A O   
1237 C CB  . GLU A 169 ? 0.3540 0.4415 0.3067 -0.0377 0.0441  0.0302  348 GLU A CB  
1238 C CG  . GLU A 169 ? 0.3725 0.4679 0.3105 -0.0460 0.0494  0.0311  348 GLU A CG  
1239 C CD  . GLU A 169 ? 0.4102 0.5025 0.3313 -0.0476 0.0439  0.0360  348 GLU A CD  
1240 O OE1 . GLU A 169 ? 0.4235 0.5075 0.3456 -0.0420 0.0356  0.0394  348 GLU A OE1 
1241 O OE2 . GLU A 169 ? 0.4274 0.5270 0.3344 -0.0548 0.0478  0.0362  348 GLU A OE2 
1242 N N   . GLY A 170 ? 0.3122 0.4182 0.2830 -0.0493 0.0594  0.0286  349 GLY A N   
1243 C CA  . GLY A 170 ? 0.3178 0.4276 0.2858 -0.0589 0.0632  0.0342  349 GLY A CA  
1244 C C   . GLY A 170 ? 0.3129 0.4195 0.2946 -0.0588 0.0605  0.0368  349 GLY A C   
1245 O O   . GLY A 170 ? 0.3251 0.4268 0.3022 -0.0664 0.0598  0.0444  349 GLY A O   
1246 N N   . LYS A 171 ? 0.2962 0.4049 0.2940 -0.0507 0.0587  0.0307  350 LYS A N   
1247 C CA  . LYS A 171 ? 0.2956 0.4045 0.3071 -0.0509 0.0563  0.0316  350 LYS A CA  
1248 C C   . LYS A 171 ? 0.2735 0.4002 0.3028 -0.0490 0.0624  0.0235  350 LYS A C   
1249 O O   . LYS A 171 ? 0.2732 0.4065 0.3067 -0.0431 0.0658  0.0164  350 LYS A O   
1250 C CB  . LYS A 171 ? 0.3169 0.4119 0.3305 -0.0437 0.0472  0.0332  350 LYS A CB  
1251 C CG  . LYS A 171 ? 0.3532 0.4320 0.3519 -0.0440 0.0412  0.0403  350 LYS A CG  
1252 C CD  . LYS A 171 ? 0.3762 0.4422 0.3781 -0.0401 0.0335  0.0425  350 LYS A CD  
1253 C CE  . LYS A 171 ? 0.4063 0.4568 0.3956 -0.0406 0.0282  0.0498  350 LYS A CE  
1254 N NZ  . LYS A 171 ? 0.4440 0.4822 0.4375 -0.0377 0.0219  0.0508  350 LYS A NZ  
1255 N N   . ALA A 172 ? 0.2529 0.3870 0.2933 -0.0540 0.0634  0.0246  351 ALA A N   
1256 C CA  . ALA A 172 ? 0.2387 0.3922 0.2985 -0.0525 0.0686  0.0177  351 ALA A CA  
1257 C C   . ALA A 172 ? 0.2335 0.3862 0.3078 -0.0424 0.0621  0.0145  351 ALA A C   
1258 O O   . ALA A 172 ? 0.2161 0.3839 0.3085 -0.0399 0.0638  0.0101  351 ALA A O   
1259 C CB  . ALA A 172 ? 0.2222 0.3857 0.2877 -0.0633 0.0721  0.0205  351 ALA A CB  
1260 N N   . GLN A 173 ? 0.2511 0.3872 0.3173 -0.0370 0.0545  0.0172  352 GLN A N   
1261 C CA  . GLN A 173 ? 0.2645 0.3980 0.3406 -0.0286 0.0480  0.0153  352 GLN A CA  
1262 C C   . GLN A 173 ? 0.2600 0.3829 0.3283 -0.0209 0.0457  0.0136  352 GLN A C   
1263 O O   . GLN A 173 ? 0.2758 0.3902 0.3295 -0.0226 0.0465  0.0153  352 GLN A O   
1264 C CB  . GLN A 173 ? 0.3155 0.4398 0.3902 -0.0314 0.0405  0.0202  352 GLN A CB  
1265 C CG  . GLN A 173 ? 0.3667 0.5030 0.4540 -0.0376 0.0408  0.0204  352 GLN A CG  
1266 C CD  . GLN A 173 ? 0.4180 0.5459 0.5057 -0.0387 0.0326  0.0228  352 GLN A CD  
1267 O OE1 . GLN A 173 ? 0.4383 0.5745 0.5382 -0.0358 0.0286  0.0208  352 GLN A OE1 
1268 N NE2 . GLN A 173 ? 0.4489 0.5601 0.5230 -0.0426 0.0299  0.0269  352 GLN A NE2 
1269 N N   . PHE A 174 ? 0.2324 0.3561 0.3108 -0.0131 0.0423  0.0108  353 PHE A N   
1270 C CA  . PHE A 174 ? 0.2362 0.3486 0.3081 -0.0068 0.0389  0.0099  353 PHE A CA  
1271 C C   . PHE A 174 ? 0.2316 0.3383 0.3071 -0.0035 0.0308  0.0126  353 PHE A C   
1272 O O   . PHE A 174 ? 0.2198 0.3335 0.3050 -0.0049 0.0282  0.0138  353 PHE A O   
1273 C CB  . PHE A 174 ? 0.2318 0.3487 0.3101 -0.0009 0.0435  0.0036  353 PHE A CB  
1274 C CG  . PHE A 174 ? 0.2328 0.3603 0.3305 0.0045  0.0433  0.0008  353 PHE A CG  
1275 C CD1 . PHE A 174 ? 0.2286 0.3726 0.3389 0.0023  0.0487  -0.0019 353 PHE A CD1 
1276 C CD2 . PHE A 174 ? 0.2360 0.3578 0.3397 0.0116  0.0374  0.0015  353 PHE A CD2 
1277 C CE1 . PHE A 174 ? 0.2224 0.3779 0.3526 0.0083  0.0477  -0.0043 353 PHE A CE1 
1278 C CE2 . PHE A 174 ? 0.2303 0.3616 0.3522 0.0174  0.0360  0.0001  353 PHE A CE2 
1279 C CZ  . PHE A 174 ? 0.2165 0.3652 0.3526 0.0163  0.0409  -0.0030 353 PHE A CZ  
1280 N N   . ALA A 175 ? 0.2413 0.3368 0.3086 0.0000  0.0270  0.0133  354 ALA A N   
1281 C CA  . ALA A 175 ? 0.2521 0.3419 0.3195 0.0020  0.0200  0.0157  354 ALA A CA  
1282 C C   . ALA A 175 ? 0.2475 0.3347 0.3186 0.0084  0.0181  0.0143  354 ALA A C   
1283 O O   . ALA A 175 ? 0.2575 0.3396 0.3235 0.0104  0.0207  0.0120  354 ALA A O   
1284 C CB  . ALA A 175 ? 0.2521 0.3313 0.3065 -0.0005 0.0172  0.0181  354 ALA A CB  
1285 N N   . ASP A 176 ? 0.2546 0.3449 0.3341 0.0108  0.0131  0.0160  355 ASP A N   
1286 C CA  . ASP A 176 ? 0.2705 0.3560 0.3522 0.0163  0.0098  0.0167  355 ASP A CA  
1287 C C   . ASP A 176 ? 0.2806 0.3588 0.3530 0.0146  0.0038  0.0201  355 ASP A C   
1288 O O   . ASP A 176 ? 0.2829 0.3650 0.3567 0.0122  -0.0006 0.0222  355 ASP A O   
1289 C CB  . ASP A 176 ? 0.2682 0.3629 0.3663 0.0211  0.0080  0.0170  355 ASP A CB  
1290 C CG  . ASP A 176 ? 0.2754 0.3760 0.3836 0.0249  0.0148  0.0120  355 ASP A CG  
1291 O OD1 . ASP A 176 ? 0.2754 0.3735 0.3762 0.0225  0.0211  0.0083  355 ASP A OD1 
1292 O OD2 . ASP A 176 ? 0.2702 0.3785 0.3939 0.0303  0.0136  0.0115  355 ASP A OD2 
1293 N N   . ILE A 177 ? 0.2778 0.3465 0.3404 0.0151  0.0041  0.0198  356 ILE A N   
1294 C CA  . ILE A 177 ? 0.2877 0.3508 0.3411 0.0131  -0.0002 0.0220  356 ILE A CA  
1295 C C   . ILE A 177 ? 0.2913 0.3495 0.3448 0.0159  -0.0032 0.0245  356 ILE A C   
1296 O O   . ILE A 177 ? 0.2895 0.3414 0.3410 0.0175  -0.0006 0.0232  356 ILE A O   
1297 C CB  . ILE A 177 ? 0.2966 0.3545 0.3391 0.0106  0.0021  0.0202  356 ILE A CB  
1298 C CG1 . ILE A 177 ? 0.3023 0.3624 0.3441 0.0086  0.0056  0.0187  356 ILE A CG1 
1299 C CG2 . ILE A 177 ? 0.3074 0.3625 0.3422 0.0084  -0.0015 0.0211  356 ILE A CG2 
1300 C CD1 . ILE A 177 ? 0.3100 0.3736 0.3544 0.0056  0.0038  0.0198  356 ILE A CD1 
1301 N N   . GLU A 178 ? 0.2923 0.3528 0.3473 0.0157  -0.0091 0.0284  357 GLU A N   
1302 C CA  . GLU A 178 ? 0.3208 0.3752 0.3732 0.0172  -0.0130 0.0325  357 GLU A CA  
1303 C C   . GLU A 178 ? 0.3053 0.3533 0.3438 0.0129  -0.0124 0.0323  357 GLU A C   
1304 O O   . GLU A 178 ? 0.2986 0.3493 0.3309 0.0094  -0.0121 0.0303  357 GLU A O   
1305 C CB  . GLU A 178 ? 0.3401 0.4004 0.3971 0.0177  -0.0202 0.0375  357 GLU A CB  
1306 C CG  . GLU A 178 ? 0.3801 0.4494 0.4536 0.0224  -0.0210 0.0375  357 GLU A CG  
1307 C CD  . GLU A 178 ? 0.4276 0.5058 0.5070 0.0226  -0.0291 0.0423  357 GLU A CD  
1308 O OE1 . GLU A 178 ? 0.4369 0.5179 0.5283 0.0286  -0.0326 0.0456  357 GLU A OE1 
1309 O OE2 . GLU A 178 ? 0.4781 0.5606 0.5503 0.0170  -0.0321 0.0424  357 GLU A OE2 
1310 N N   . PRO A 179 ? 0.3057 0.3451 0.3398 0.0131  -0.0120 0.0340  358 PRO A N   
1311 C CA  . PRO A 179 ? 0.3076 0.3432 0.3298 0.0084  -0.0107 0.0334  358 PRO A CA  
1312 C C   . PRO A 179 ? 0.3228 0.3597 0.3370 0.0045  -0.0155 0.0376  358 PRO A C   
1313 O O   . PRO A 179 ? 0.3073 0.3384 0.3145 0.0018  -0.0167 0.0412  358 PRO A O   
1314 C CB  . PRO A 179 ? 0.3004 0.3264 0.3223 0.0092  -0.0085 0.0336  358 PRO A CB  
1315 C CG  . PRO A 179 ? 0.3033 0.3256 0.3350 0.0145  -0.0115 0.0373  358 PRO A CG  
1316 C CD  . PRO A 179 ? 0.2993 0.3322 0.3405 0.0176  -0.0124 0.0360  358 PRO A CD  
1317 N N   . LYS A 180 ? 0.3414 0.3859 0.3559 0.0034  -0.0179 0.0368  359 LYS A N   
1318 C CA  . LYS A 180 ? 0.3547 0.4026 0.3621 -0.0004 -0.0229 0.0400  359 LYS A CA  
1319 C C   . LYS A 180 ? 0.3397 0.3874 0.3345 -0.0059 -0.0205 0.0377  359 LYS A C   
1320 O O   . LYS A 180 ? 0.3169 0.3656 0.3107 -0.0063 -0.0157 0.0319  359 LYS A O   
1321 C CB  . LYS A 180 ? 0.3918 0.4480 0.4033 -0.0010 -0.0252 0.0377  359 LYS A CB  
1322 C CG  . LYS A 180 ? 0.4635 0.5249 0.4840 0.0014  -0.0312 0.0423  359 LYS A CG  
1323 C CD  . LYS A 180 ? 0.4860 0.5562 0.5110 -0.0005 -0.0329 0.0391  359 LYS A CD  
1324 C CE  . LYS A 180 ? 0.5059 0.5778 0.5194 -0.0067 -0.0333 0.0352  359 LYS A CE  
1325 N NZ  . LYS A 180 ? 0.5256 0.6006 0.5301 -0.0106 -0.0396 0.0396  359 LYS A NZ  
1326 N N   . PHE A 181 ? 0.3364 0.3843 0.3219 -0.0103 -0.0242 0.0423  360 PHE A N   
1327 C CA  . PHE A 181 ? 0.3405 0.3909 0.3135 -0.0165 -0.0218 0.0398  360 PHE A CA  
1328 C C   . PHE A 181 ? 0.3272 0.3842 0.3001 -0.0171 -0.0189 0.0313  360 PHE A C   
1329 O O   . PHE A 181 ? 0.3170 0.3776 0.2929 -0.0165 -0.0217 0.0298  360 PHE A O   
1330 C CB  . PHE A 181 ? 0.3522 0.4038 0.3144 -0.0218 -0.0272 0.0463  360 PHE A CB  
1331 C CG  . PHE A 181 ? 0.3643 0.4206 0.3125 -0.0293 -0.0242 0.0434  360 PHE A CG  
1332 C CD1 . PHE A 181 ? 0.3770 0.4300 0.3189 -0.0333 -0.0202 0.0447  360 PHE A CD1 
1333 C CD2 . PHE A 181 ? 0.3745 0.4392 0.3162 -0.0330 -0.0248 0.0384  360 PHE A CD2 
1334 C CE1 . PHE A 181 ? 0.3849 0.4447 0.3148 -0.0407 -0.0165 0.0414  360 PHE A CE1 
1335 C CE2 . PHE A 181 ? 0.3722 0.4426 0.3015 -0.0399 -0.0210 0.0344  360 PHE A CE2 
1336 C CZ  . PHE A 181 ? 0.3865 0.4553 0.3102 -0.0437 -0.0166 0.0360  360 PHE A CZ  
1337 N N   . ASP A 182 ? 0.3134 0.3717 0.2838 -0.0181 -0.0133 0.0257  361 ASP A N   
1338 C CA  . ASP A 182 ? 0.3160 0.3794 0.2856 -0.0184 -0.0101 0.0174  361 ASP A CA  
1339 C C   . ASP A 182 ? 0.3079 0.3694 0.2874 -0.0133 -0.0100 0.0143  361 ASP A C   
1340 O O   . ASP A 182 ? 0.2975 0.3606 0.2773 -0.0133 -0.0094 0.0086  361 ASP A O   
1341 C CB  . ASP A 182 ? 0.3240 0.3929 0.2835 -0.0240 -0.0117 0.0152  361 ASP A CB  
1342 C CG  . ASP A 182 ? 0.3356 0.4093 0.2935 -0.0245 -0.0072 0.0052  361 ASP A CG  
1343 O OD1 . ASP A 182 ? 0.3243 0.3996 0.2852 -0.0225 -0.0024 0.0012  361 ASP A OD1 
1344 O OD2 . ASP A 182 ? 0.3459 0.4221 0.3001 -0.0268 -0.0088 0.0010  361 ASP A OD2 
1345 N N   . ARG A 183 ? 0.2981 0.3555 0.2853 -0.0094 -0.0101 0.0177  362 ARG A N   
1346 C CA  . ARG A 183 ? 0.2810 0.3369 0.2765 -0.0055 -0.0094 0.0158  362 ARG A CA  
1347 C C   . ARG A 183 ? 0.2761 0.3308 0.2735 -0.0030 -0.0053 0.0126  362 ARG A C   
1348 O O   . ARG A 183 ? 0.2834 0.3375 0.2799 -0.0029 -0.0034 0.0137  362 ARG A O   
1349 C CB  . ARG A 183 ? 0.2712 0.3256 0.2741 -0.0032 -0.0116 0.0207  362 ARG A CB  
1350 C CG  . ARG A 183 ? 0.2713 0.3248 0.2819 -0.0002 -0.0095 0.0193  362 ARG A CG  
1351 C CD  . ARG A 183 ? 0.2799 0.3349 0.2990 0.0018  -0.0111 0.0228  362 ARG A CD  
1352 N NE  . ARG A 183 ? 0.2773 0.3371 0.2991 -0.0001 -0.0151 0.0237  362 ARG A NE  
1353 C CZ  . ARG A 183 ? 0.2851 0.3496 0.3160 0.0012  -0.0175 0.0263  362 ARG A CZ  
1354 N NH1 . ARG A 183 ? 0.2876 0.3580 0.3209 -0.0016 -0.0215 0.0265  362 ARG A NH1 
1355 N NH2 . ARG A 183 ? 0.2723 0.3366 0.3106 0.0052  -0.0156 0.0280  362 ARG A NH2 
1356 N N   . LEU A 184 ? 0.2732 0.3271 0.2733 -0.0011 -0.0043 0.0088  363 LEU A N   
1357 C CA  . LEU A 184 ? 0.2779 0.3311 0.2805 0.0020  -0.0018 0.0068  363 LEU A CA  
1358 C C   . LEU A 184 ? 0.2838 0.3334 0.2913 0.0041  -0.0020 0.0091  363 LEU A C   
1359 O O   . LEU A 184 ? 0.2994 0.3471 0.3091 0.0032  -0.0035 0.0097  363 LEU A O   
1360 C CB  . LEU A 184 ? 0.2772 0.3316 0.2788 0.0030  -0.0009 0.0012  363 LEU A CB  
1361 C CG  . LEU A 184 ? 0.2788 0.3342 0.2837 0.0071  0.0007  -0.0008 363 LEU A CG  
1362 C CD1 . LEU A 184 ? 0.2773 0.3394 0.2808 0.0060  0.0026  -0.0014 363 LEU A CD1 
1363 C CD2 . LEU A 184 ? 0.2739 0.3281 0.2806 0.0097  0.0009  -0.0064 363 LEU A CD2 
1364 N N   . LEU A 185 ? 0.2809 0.3304 0.2896 0.0060  -0.0004 0.0101  364 LEU A N   
1365 C CA  . LEU A 185 ? 0.2842 0.3315 0.2959 0.0069  0.0002  0.0124  364 LEU A CA  
1366 C C   . LEU A 185 ? 0.2962 0.3431 0.3068 0.0090  0.0009  0.0120  364 LEU A C   
1367 O O   . LEU A 185 ? 0.2959 0.3463 0.3051 0.0097  0.0015  0.0105  364 LEU A O   
1368 C CB  . LEU A 185 ? 0.2850 0.3333 0.2986 0.0065  0.0015  0.0145  364 LEU A CB  
1369 C CG  . LEU A 185 ? 0.2873 0.3356 0.3031 0.0069  0.0036  0.0156  364 LEU A CG  
1370 C CD1 . LEU A 185 ? 0.2865 0.3348 0.3062 0.0057  0.0031  0.0172  364 LEU A CD1 
1371 C CD2 . LEU A 185 ? 0.2789 0.3281 0.2966 0.0073  0.0056  0.0155  364 LEU A CD2 
1372 N N   . PHE A 186 ? 0.2874 0.3304 0.2987 0.0095  0.0004  0.0138  365 PHE A N   
1373 C CA  . PHE A 186 ? 0.3003 0.3423 0.3099 0.0114  0.0000  0.0154  365 PHE A CA  
1374 C C   . PHE A 186 ? 0.2997 0.3408 0.3082 0.0092  0.0015  0.0190  365 PHE A C   
1375 O O   . PHE A 186 ? 0.2877 0.3271 0.2983 0.0068  0.0022  0.0202  365 PHE A O   
1376 C CB  . PHE A 186 ? 0.3137 0.3497 0.3241 0.0137  -0.0023 0.0154  365 PHE A CB  
1377 C CG  . PHE A 186 ? 0.3246 0.3617 0.3370 0.0162  -0.0031 0.0106  365 PHE A CG  
1378 C CD1 . PHE A 186 ? 0.3392 0.3749 0.3520 0.0143  -0.0028 0.0074  365 PHE A CD1 
1379 C CD2 . PHE A 186 ? 0.3341 0.3753 0.3480 0.0202  -0.0039 0.0087  365 PHE A CD2 
1380 C CE1 . PHE A 186 ? 0.3472 0.3848 0.3607 0.0159  -0.0026 0.0019  365 PHE A CE1 
1381 C CE2 . PHE A 186 ? 0.3408 0.3849 0.3575 0.0225  -0.0036 0.0032  365 PHE A CE2 
1382 C CZ  . PHE A 186 ? 0.3385 0.3805 0.3544 0.0202  -0.0025 -0.0005 365 PHE A CZ  
1383 N N   . PHE A 187 ? 0.3064 0.3501 0.3113 0.0094  0.0020  0.0203  366 PHE A N   
1384 C CA  . PHE A 187 ? 0.3027 0.3462 0.3043 0.0068  0.0037  0.0235  366 PHE A CA  
1385 C C   . PHE A 187 ? 0.3078 0.3533 0.3036 0.0074  0.0021  0.0255  366 PHE A C   
1386 O O   . PHE A 187 ? 0.3112 0.3607 0.3069 0.0096  0.0006  0.0233  366 PHE A O   
1387 C CB  . PHE A 187 ? 0.3049 0.3526 0.3087 0.0045  0.0077  0.0216  366 PHE A CB  
1388 C CG  . PHE A 187 ? 0.3018 0.3533 0.3054 0.0052  0.0092  0.0179  366 PHE A CG  
1389 C CD1 . PHE A 187 ? 0.3054 0.3601 0.3037 0.0039  0.0108  0.0169  366 PHE A CD1 
1390 C CD2 . PHE A 187 ? 0.2916 0.3428 0.2992 0.0063  0.0089  0.0157  366 PHE A CD2 
1391 C CE1 . PHE A 187 ? 0.3039 0.3605 0.3018 0.0036  0.0123  0.0128  366 PHE A CE1 
1392 C CE2 . PHE A 187 ? 0.2962 0.3486 0.3032 0.0061  0.0103  0.0128  366 PHE A CE2 
1393 C CZ  . PHE A 187 ? 0.3029 0.3575 0.3055 0.0047  0.0121  0.0110  366 PHE A CZ  
1394 N N   . TRP A 188 ? 0.3039 0.3474 0.2944 0.0049  0.0022  0.0302  367 TRP A N   
1395 C CA  . TRP A 188 ? 0.3118 0.3582 0.2951 0.0047  0.0002  0.0330  367 TRP A CA  
1396 C C   . TRP A 188 ? 0.3117 0.3665 0.2926 0.0030  0.0030  0.0283  367 TRP A C   
1397 O O   . TRP A 188 ? 0.3094 0.3660 0.2913 0.0004  0.0078  0.0251  367 TRP A O   
1398 C CB  . TRP A 188 ? 0.3172 0.3601 0.2931 0.0006  0.0005  0.0395  367 TRP A CB  
1399 C CG  . TRP A 188 ? 0.3179 0.3502 0.2950 0.0006  -0.0019 0.0447  367 TRP A CG  
1400 C CD1 . TRP A 188 ? 0.3141 0.3424 0.2900 -0.0046 0.0010  0.0477  367 TRP A CD1 
1401 C CD2 . TRP A 188 ? 0.3215 0.3455 0.3016 0.0058  -0.0073 0.0471  367 TRP A CD2 
1402 N NE1 . TRP A 188 ? 0.3192 0.3356 0.2962 -0.0039 -0.0025 0.0521  367 TRP A NE1 
1403 C CE2 . TRP A 188 ? 0.3278 0.3407 0.3076 0.0030  -0.0076 0.0515  367 TRP A CE2 
1404 C CE3 . TRP A 188 ? 0.3309 0.3562 0.3149 0.0123  -0.0117 0.0453  367 TRP A CE3 
1405 C CZ2 . TRP A 188 ? 0.3369 0.3377 0.3197 0.0071  -0.0121 0.0538  367 TRP A CZ2 
1406 C CZ3 . TRP A 188 ? 0.3419 0.3574 0.3300 0.0171  -0.0159 0.0473  367 TRP A CZ3 
1407 C CH2 . TRP A 188 ? 0.3430 0.3451 0.3302 0.0147  -0.0162 0.0514  367 TRP A CH2 
1408 N N   . SER A 189 ? 0.3076 0.3673 0.2860 0.0044  -0.0003 0.0276  368 SER A N   
1409 C CA  . SER A 189 ? 0.3085 0.3753 0.2847 0.0022  0.0018  0.0222  368 SER A CA  
1410 C C   . SER A 189 ? 0.3087 0.3794 0.2755 -0.0027 0.0042  0.0224  368 SER A C   
1411 O O   . SER A 189 ? 0.3151 0.3897 0.2797 -0.0055 0.0075  0.0167  368 SER A O   
1412 C CB  . SER A 189 ? 0.3013 0.3741 0.2794 0.0046  -0.0026 0.0209  368 SER A CB  
1413 O OG  . SER A 189 ? 0.3085 0.3794 0.2950 0.0084  -0.0036 0.0193  368 SER A OG  
1414 N N   . ASP A 190 ? 0.3204 0.3892 0.2805 -0.0042 0.0026  0.0289  369 ASP A N   
1415 C CA  . ASP A 190 ? 0.3323 0.4062 0.2808 -0.0097 0.0044  0.0297  369 ASP A CA  
1416 C C   . ASP A 190 ? 0.3396 0.4137 0.2877 -0.0137 0.0124  0.0261  369 ASP A C   
1417 O O   . ASP A 190 ? 0.3227 0.3941 0.2805 -0.0117 0.0158  0.0222  369 ASP A O   
1418 C CB  . ASP A 190 ? 0.3318 0.4045 0.2717 -0.0104 -0.0014 0.0391  369 ASP A CB  
1419 C CG  . ASP A 190 ? 0.3421 0.4055 0.2821 -0.0109 -0.0011 0.0462  369 ASP A CG  
1420 O OD1 . ASP A 190 ? 0.3324 0.3923 0.2795 -0.0112 0.0037  0.0433  369 ASP A OD1 
1421 O OD2 . ASP A 190 ? 0.3379 0.3974 0.2709 -0.0113 -0.0063 0.0549  369 ASP A OD2 
1422 N N   . ARG A 191 ? 0.3419 0.4204 0.2788 -0.0195 0.0151  0.0274  370 ARG A N   
1423 C CA  . ARG A 191 ? 0.3475 0.4298 0.2835 -0.0237 0.0237  0.0221  370 ARG A CA  
1424 C C   . ARG A 191 ? 0.3315 0.4102 0.2754 -0.0235 0.0268  0.0250  370 ARG A C   
1425 O O   . ARG A 191 ? 0.3360 0.4191 0.2837 -0.0257 0.0340  0.0200  370 ARG A O   
1426 C CB  . ARG A 191 ? 0.3769 0.4664 0.2973 -0.0309 0.0260  0.0228  370 ARG A CB  
1427 C CG  . ARG A 191 ? 0.4190 0.5060 0.3293 -0.0343 0.0220  0.0344  370 ARG A CG  
1428 C CD  . ARG A 191 ? 0.4879 0.5812 0.3865 -0.0429 0.0288  0.0348  370 ARG A CD  
1429 N NE  . ARG A 191 ? 0.5275 0.6307 0.4159 -0.0477 0.0332  0.0268  370 ARG A NE  
1430 C CZ  . ARG A 191 ? 0.5536 0.6648 0.4336 -0.0549 0.0417  0.0227  370 ARG A CZ  
1431 N NH1 . ARG A 191 ? 0.5727 0.6844 0.4550 -0.0583 0.0471  0.0260  370 ARG A NH1 
1432 N NH2 . ARG A 191 ? 0.5748 0.6943 0.4445 -0.0593 0.0453  0.0145  370 ARG A NH2 
1433 N N   . ARG A 192 ? 0.3172 0.3882 0.2643 -0.0210 0.0214  0.0323  371 ARG A N   
1434 C CA  . ARG A 192 ? 0.3212 0.3883 0.2761 -0.0216 0.0234  0.0348  371 ARG A CA  
1435 C C   . ARG A 192 ? 0.3056 0.3742 0.2743 -0.0178 0.0265  0.0277  371 ARG A C   
1436 O O   . ARG A 192 ? 0.3058 0.3761 0.2817 -0.0192 0.0300  0.0273  371 ARG A O   
1437 C CB  . ARG A 192 ? 0.3366 0.3934 0.2920 -0.0194 0.0166  0.0427  371 ARG A CB  
1438 C CG  . ARG A 192 ? 0.3645 0.4175 0.3073 -0.0239 0.0137  0.0520  371 ARG A CG  
1439 C CD  . ARG A 192 ? 0.3767 0.4171 0.3210 -0.0202 0.0064  0.0593  371 ARG A CD  
1440 N NE  . ARG A 192 ? 0.3931 0.4329 0.3397 -0.0130 0.0001  0.0582  371 ARG A NE  
1441 C CZ  . ARG A 192 ? 0.3914 0.4219 0.3410 -0.0078 -0.0066 0.0628  371 ARG A CZ  
1442 N NH1 . ARG A 192 ? 0.4049 0.4233 0.3545 -0.0092 -0.0081 0.0690  371 ARG A NH1 
1443 N NH2 . ARG A 192 ? 0.3952 0.4288 0.3485 -0.0014 -0.0114 0.0607  371 ARG A NH2 
1444 N N   . ASN A 193 ? 0.2930 0.3615 0.2653 -0.0133 0.0249  0.0226  372 ASN A N   
1445 C CA  . ASN A 193 ? 0.2935 0.3615 0.2779 -0.0095 0.0263  0.0178  372 ASN A CA  
1446 C C   . ASN A 193 ? 0.2949 0.3658 0.2805 -0.0083 0.0297  0.0103  372 ASN A C   
1447 O O   . ASN A 193 ? 0.2991 0.3668 0.2866 -0.0055 0.0268  0.0083  372 ASN A O   
1448 C CB  . ASN A 193 ? 0.2922 0.3539 0.2818 -0.0053 0.0206  0.0202  372 ASN A CB  
1449 C CG  . ASN A 193 ? 0.2973 0.3546 0.2893 -0.0062 0.0184  0.0254  372 ASN A CG  
1450 O OD1 . ASN A 193 ? 0.2943 0.3538 0.2919 -0.0083 0.0214  0.0253  372 ASN A OD1 
1451 N ND2 . ASN A 193 ? 0.2892 0.3404 0.2781 -0.0046 0.0133  0.0293  372 ASN A ND2 
1452 N N   . PRO A 194 ? 0.2966 0.3731 0.2817 -0.0107 0.0363  0.0053  373 PRO A N   
1453 C CA  . PRO A 194 ? 0.2939 0.3706 0.2835 -0.0086 0.0400  -0.0029 373 PRO A CA  
1454 C C   . PRO A 194 ? 0.2939 0.3670 0.2973 -0.0034 0.0388  -0.0033 373 PRO A C   
1455 O O   . PRO A 194 ? 0.2949 0.3699 0.3052 -0.0027 0.0384  0.0002  373 PRO A O   
1456 C CB  . PRO A 194 ? 0.2958 0.3803 0.2840 -0.0118 0.0480  -0.0083 373 PRO A CB  
1457 C CG  . PRO A 194 ? 0.3004 0.3891 0.2779 -0.0176 0.0477  -0.0020 373 PRO A CG  
1458 C CD  . PRO A 194 ? 0.2956 0.3784 0.2759 -0.0158 0.0410  0.0067  373 PRO A CD  
1459 N N   . HIS A 195 ? 0.2975 0.3651 0.3041 -0.0005 0.0379  -0.0070 374 HIS A N   
1460 C CA  . HIS A 195 ? 0.3064 0.3695 0.3238 0.0042  0.0354  -0.0058 374 HIS A CA  
1461 C C   . HIS A 195 ? 0.3194 0.3762 0.3402 0.0065  0.0370  -0.0114 374 HIS A C   
1462 O O   . HIS A 195 ? 0.3226 0.3772 0.3360 0.0039  0.0386  -0.0158 374 HIS A O   
1463 C CB  . HIS A 195 ? 0.3028 0.3623 0.3186 0.0046  0.0288  0.0002  374 HIS A CB  
1464 C CG  . HIS A 195 ? 0.3024 0.3593 0.3094 0.0027  0.0260  0.0003  374 HIS A CG  
1465 N ND1 . HIS A 195 ? 0.3000 0.3603 0.2980 -0.0001 0.0251  0.0017  374 HIS A ND1 
1466 C CD2 . HIS A 195 ? 0.3006 0.3529 0.3070 0.0031  0.0237  -0.0006 374 HIS A CD2 
1467 C CE1 . HIS A 195 ? 0.2981 0.3575 0.2920 -0.0008 0.0221  0.0012  374 HIS A CE1 
1468 N NE2 . HIS A 195 ? 0.2956 0.3504 0.2943 0.0006  0.0217  -0.0005 374 HIS A NE2 
1469 N N   . GLU A 196 ? 0.3250 0.3785 0.3569 0.0112  0.0359  -0.0107 375 GLU A N   
1470 C CA  . GLU A 196 ? 0.3370 0.3819 0.3738 0.0143  0.0368  -0.0146 375 GLU A CA  
1471 C C   . GLU A 196 ? 0.3320 0.3709 0.3747 0.0175  0.0310  -0.0087 375 GLU A C   
1472 O O   . GLU A 196 ? 0.3391 0.3831 0.3865 0.0189  0.0278  -0.0036 375 GLU A O   
1473 C CB  . GLU A 196 ? 0.3441 0.3921 0.3904 0.0178  0.0431  -0.0214 375 GLU A CB  
1474 C CG  . GLU A 196 ? 0.3745 0.4296 0.4350 0.0226  0.0424  -0.0185 375 GLU A CG  
1475 C CD  . GLU A 196 ? 0.3933 0.4564 0.4650 0.0260  0.0495  -0.0257 375 GLU A CD  
1476 O OE1 . GLU A 196 ? 0.4096 0.4791 0.4958 0.0309  0.0485  -0.0239 375 GLU A OE1 
1477 O OE2 . GLU A 196 ? 0.4150 0.4795 0.4813 0.0236  0.0560  -0.0334 375 GLU A OE2 
1478 N N   . VAL A 197 ? 0.3482 0.3760 0.3895 0.0178  0.0295  -0.0092 376 VAL A N   
1479 C CA  . VAL A 197 ? 0.3473 0.3683 0.3935 0.0207  0.0243  -0.0033 376 VAL A CA  
1480 C C   . VAL A 197 ? 0.3614 0.3765 0.4197 0.0271  0.0258  -0.0058 376 VAL A C   
1481 O O   . VAL A 197 ? 0.3588 0.3653 0.4169 0.0274  0.0295  -0.0118 376 VAL A O   
1482 C CB  . VAL A 197 ? 0.3652 0.3776 0.4020 0.0162  0.0213  -0.0008 376 VAL A CB  
1483 C CG1 . VAL A 197 ? 0.3635 0.3684 0.4031 0.0181  0.0159  0.0061  376 VAL A CG1 
1484 C CG2 . VAL A 197 ? 0.3577 0.3775 0.3850 0.0113  0.0200  0.0007  376 VAL A CG2 
1485 N N   . GLN A 198 ? 0.3620 0.3822 0.4314 0.0322  0.0227  -0.0017 377 GLN A N   
1486 C CA  . GLN A 198 ? 0.3794 0.3958 0.4634 0.0399  0.0226  -0.0027 377 GLN A CA  
1487 C C   . GLN A 198 ? 0.3643 0.3630 0.4460 0.0410  0.0186  0.0010  377 GLN A C   
1488 O O   . GLN A 198 ? 0.3559 0.3496 0.4267 0.0358  0.0145  0.0066  377 GLN A O   
1489 C CB  . GLN A 198 ? 0.4120 0.4397 0.5078 0.0442  0.0182  0.0026  377 GLN A CB  
1490 C CG  . GLN A 198 ? 0.4616 0.5064 0.5617 0.0428  0.0223  -0.0006 377 GLN A CG  
1491 C CD  . GLN A 198 ? 0.4977 0.5493 0.6107 0.0477  0.0293  -0.0087 377 GLN A CD  
1492 O OE1 . GLN A 198 ? 0.5312 0.5819 0.6594 0.0556  0.0284  -0.0096 377 GLN A OE1 
1493 N NE2 . GLN A 198 ? 0.5160 0.5752 0.6235 0.0431  0.0365  -0.0148 377 GLN A NE2 
1494 N N   . PRO A 199 ? 0.3575 0.3460 0.4498 0.0475  0.0198  -0.0021 378 PRO A N   
1495 C CA  . PRO A 199 ? 0.3599 0.3287 0.4498 0.0482  0.0158  0.0022  378 PRO A CA  
1496 C C   . PRO A 199 ? 0.3467 0.3139 0.4329 0.0470  0.0069  0.0145  378 PRO A C   
1497 O O   . PRO A 199 ? 0.3444 0.3226 0.4386 0.0510  0.0025  0.0195  378 PRO A O   
1498 C CB  . PRO A 199 ? 0.3628 0.3246 0.4700 0.0584  0.0173  -0.0018 378 PRO A CB  
1499 C CG  . PRO A 199 ? 0.3615 0.3374 0.4752 0.0601  0.0259  -0.0132 378 PRO A CG  
1500 C CD  . PRO A 199 ? 0.3605 0.3553 0.4678 0.0546  0.0255  -0.0102 378 PRO A CD  
1501 N N   . ALA A 200 ? 0.3489 0.3035 0.4221 0.0404  0.0045  0.0190  379 ALA A N   
1502 C CA  . ALA A 200 ? 0.3592 0.3114 0.4256 0.0375  -0.0032 0.0302  379 ALA A CA  
1503 C C   . ALA A 200 ? 0.3721 0.3044 0.4414 0.0409  -0.0079 0.0368  379 ALA A C   
1504 O O   . ALA A 200 ? 0.3797 0.2958 0.4480 0.0402  -0.0045 0.0327  379 ALA A O   
1505 C CB  . ALA A 200 ? 0.3663 0.3206 0.4161 0.0271  -0.0020 0.0308  379 ALA A CB  
1506 N N   . TYR A 201 ? 0.3855 0.3186 0.4578 0.0443  -0.0162 0.0474  380 TYR A N   
1507 C CA  . TYR A 201 ? 0.4085 0.3228 0.4842 0.0486  -0.0225 0.0560  380 TYR A CA  
1508 C C   . TYR A 201 ? 0.4131 0.3229 0.4730 0.0405  -0.0292 0.0681  380 TYR A C   
1509 O O   . TYR A 201 ? 0.4180 0.3153 0.4784 0.0432  -0.0368 0.0788  380 TYR A O   
1510 C CB  . TYR A 201 ? 0.4096 0.3285 0.5059 0.0616  -0.0266 0.0574  380 TYR A CB  
1511 C CG  . TYR A 201 ? 0.4209 0.3425 0.5322 0.0688  -0.0185 0.0445  380 TYR A CG  
1512 C CD1 . TYR A 201 ? 0.4379 0.3394 0.5533 0.0720  -0.0145 0.0389  380 TYR A CD1 
1513 C CD2 . TYR A 201 ? 0.4213 0.3653 0.5413 0.0712  -0.0143 0.0372  380 TYR A CD2 
1514 C CE1 . TYR A 201 ? 0.4483 0.3532 0.5763 0.0780  -0.0062 0.0256  380 TYR A CE1 
1515 C CE2 . TYR A 201 ? 0.4280 0.3760 0.5601 0.0766  -0.0060 0.0251  380 TYR A CE2 
1516 C CZ  . TYR A 201 ? 0.4469 0.3760 0.5829 0.0802  -0.0017 0.0188  380 TYR A CZ  
1517 O OH  . TYR A 201 ? 0.4631 0.3971 0.6102 0.0851  0.0072  0.0055  380 TYR A OH  
1518 N N   . ALA A 202 ? 0.4054 0.3257 0.4513 0.0307  -0.0263 0.0662  381 ALA A N   
1519 C CA  . ALA A 202 ? 0.4068 0.3242 0.4354 0.0207  -0.0296 0.0744  381 ALA A CA  
1520 C C   . ALA A 202 ? 0.4021 0.3253 0.4196 0.0111  -0.0222 0.0667  381 ALA A C   
1521 O O   . ALA A 202 ? 0.3873 0.3201 0.4100 0.0129  -0.0163 0.0566  381 ALA A O   
1522 C CB  . ALA A 202 ? 0.4108 0.3430 0.4370 0.0207  -0.0364 0.0815  381 ALA A CB  
1523 N N   . THR A 203 ? 0.3976 0.3159 0.4001 0.0010  -0.0226 0.0717  382 THR A N   
1524 C CA  . THR A 203 ? 0.3949 0.3209 0.3883 -0.0080 -0.0162 0.0648  382 THR A CA  
1525 C C   . THR A 203 ? 0.3641 0.3119 0.3586 -0.0069 -0.0146 0.0595  382 THR A C   
1526 O O   . THR A 203 ? 0.3626 0.3193 0.3539 -0.0069 -0.0189 0.0645  382 THR A O   
1527 C CB  . THR A 203 ? 0.4170 0.3366 0.3951 -0.0195 -0.0169 0.0716  382 THR A CB  
1528 O OG1 . THR A 203 ? 0.4222 0.3187 0.3998 -0.0202 -0.0191 0.0776  382 THR A OG1 
1529 C CG2 . THR A 203 ? 0.4159 0.3448 0.3872 -0.0284 -0.0101 0.0639  382 THR A CG2 
1530 N N   . ARG A 204 ? 0.3457 0.3010 0.3439 -0.0063 -0.0086 0.0495  383 ARG A N   
1531 C CA  . ARG A 204 ? 0.3353 0.3081 0.3361 -0.0042 -0.0070 0.0442  383 ARG A CA  
1532 C C   . ARG A 204 ? 0.3285 0.3095 0.3221 -0.0110 -0.0023 0.0384  383 ARG A C   
1533 O O   . ARG A 204 ? 0.3222 0.2997 0.3162 -0.0131 0.0017  0.0330  383 ARG A O   
1534 C CB  . ARG A 204 ? 0.3266 0.3015 0.3397 0.0039  -0.0048 0.0385  383 ARG A CB  
1535 C CG  . ARG A 204 ? 0.3208 0.3115 0.3370 0.0060  -0.0034 0.0341  383 ARG A CG  
1536 C CD  . ARG A 204 ? 0.3119 0.3040 0.3382 0.0118  0.0003  0.0280  383 ARG A CD  
1537 N NE  . ARG A 204 ? 0.2891 0.2945 0.3191 0.0138  0.0017  0.0247  383 ARG A NE  
1538 C CZ  . ARG A 204 ? 0.2874 0.3003 0.3125 0.0107  0.0047  0.0205  383 ARG A CZ  
1539 N NH1 . ARG A 204 ? 0.2870 0.2982 0.3039 0.0056  0.0064  0.0186  383 ARG A NH1 
1540 N NH2 . ARG A 204 ? 0.2749 0.2971 0.3037 0.0125  0.0056  0.0187  383 ARG A NH2 
1541 N N   . TYR A 205 ? 0.3259 0.3186 0.3138 -0.0142 -0.0030 0.0390  384 TYR A N   
1542 C CA  . TYR A 205 ? 0.3352 0.3380 0.3185 -0.0193 0.0010  0.0335  384 TYR A CA  
1543 C C   . TYR A 205 ? 0.3282 0.3437 0.3159 -0.0149 0.0018  0.0286  384 TYR A C   
1544 O O   . TYR A 205 ? 0.3311 0.3498 0.3214 -0.0111 -0.0011 0.0306  384 TYR A O   
1545 C CB  . TYR A 205 ? 0.3494 0.3560 0.3227 -0.0270 0.0006  0.0370  384 TYR A CB  
1546 C CG  . TYR A 205 ? 0.3755 0.3699 0.3420 -0.0339 0.0003  0.0425  384 TYR A CG  
1547 C CD1 . TYR A 205 ? 0.3958 0.3841 0.3623 -0.0383 0.0038  0.0393  384 TYR A CD1 
1548 C CD2 . TYR A 205 ? 0.3823 0.3709 0.3414 -0.0369 -0.0038 0.0514  384 TYR A CD2 
1549 C CE1 . TYR A 205 ? 0.4036 0.3789 0.3634 -0.0457 0.0036  0.0446  384 TYR A CE1 
1550 C CE2 . TYR A 205 ? 0.4094 0.3850 0.3610 -0.0440 -0.0044 0.0578  384 TYR A CE2 
1551 C CZ  . TYR A 205 ? 0.4188 0.3869 0.3710 -0.0485 -0.0005 0.0544  384 TYR A CZ  
1552 O OH  . TYR A 205 ? 0.4678 0.4212 0.4124 -0.0566 -0.0010 0.0609  384 TYR A OH  
1553 N N   . ALA A 206 ? 0.3263 0.3488 0.3147 -0.0160 0.0052  0.0225  385 ALA A N   
1554 C CA  . ALA A 206 ? 0.3216 0.3547 0.3131 -0.0126 0.0058  0.0184  385 ALA A CA  
1555 C C   . ALA A 206 ? 0.3092 0.3513 0.2988 -0.0161 0.0084  0.0138  385 ALA A C   
1556 O O   . ALA A 206 ? 0.3117 0.3521 0.2994 -0.0208 0.0102  0.0125  385 ALA A O   
1557 C CB  . ALA A 206 ? 0.3219 0.3532 0.3196 -0.0072 0.0063  0.0165  385 ALA A CB  
1558 N N   . ILE A 207 ? 0.2974 0.3491 0.2885 -0.0137 0.0083  0.0111  386 ILE A N   
1559 C CA  . ILE A 207 ? 0.2891 0.3515 0.2813 -0.0150 0.0101  0.0065  386 ILE A CA  
1560 C C   . ILE A 207 ? 0.2834 0.3496 0.2804 -0.0090 0.0091  0.0043  386 ILE A C   
1561 O O   . ILE A 207 ? 0.2799 0.3454 0.2783 -0.0053 0.0077  0.0050  386 ILE A O   
1562 C CB  . ILE A 207 ? 0.2857 0.3564 0.2752 -0.0182 0.0112  0.0051  386 ILE A CB  
1563 C CG1 . ILE A 207 ? 0.2925 0.3588 0.2751 -0.0254 0.0120  0.0088  386 ILE A CG1 
1564 C CG2 . ILE A 207 ? 0.2714 0.3555 0.2652 -0.0180 0.0129  -0.0003 386 ILE A CG2 
1565 C CD1 . ILE A 207 ? 0.2966 0.3715 0.2745 -0.0296 0.0136  0.0076  386 ILE A CD1 
1566 N N   . THR A 208 ? 0.2746 0.3446 0.2733 -0.0090 0.0095  0.0020  387 THR A N   
1567 C CA  . THR A 208 ? 0.2783 0.3508 0.2798 -0.0041 0.0080  0.0014  387 THR A CA  
1568 C C   . THR A 208 ? 0.2744 0.3587 0.2788 -0.0033 0.0072  -0.0016 387 THR A C   
1569 O O   . THR A 208 ? 0.2664 0.3572 0.2709 -0.0076 0.0081  -0.0040 387 THR A O   
1570 C CB  . THR A 208 ? 0.2846 0.3514 0.2846 -0.0043 0.0086  0.0019  387 THR A CB  
1571 O OG1 . THR A 208 ? 0.2982 0.3553 0.2979 -0.0041 0.0094  0.0042  387 THR A OG1 
1572 C CG2 . THR A 208 ? 0.2906 0.3596 0.2913 -0.0006 0.0072  0.0025  387 THR A CG2 
1573 N N   . VAL A 209 ? 0.2644 0.3514 0.2722 0.0022  0.0051  -0.0013 388 VAL A N   
1574 C CA  . VAL A 209 ? 0.2751 0.3722 0.2870 0.0051  0.0028  -0.0029 388 VAL A CA  
1575 C C   . VAL A 209 ? 0.2829 0.3753 0.2936 0.0090  0.0000  0.0006  388 VAL A C   
1576 O O   . VAL A 209 ? 0.2792 0.3619 0.2879 0.0104  0.0003  0.0033  388 VAL A O   
1577 C CB  . VAL A 209 ? 0.2833 0.3886 0.3015 0.0087  0.0026  -0.0060 388 VAL A CB  
1578 C CG1 . VAL A 209 ? 0.2976 0.4095 0.3157 0.0035  0.0061  -0.0094 388 VAL A CG1 
1579 C CG2 . VAL A 209 ? 0.2968 0.3940 0.3160 0.0138  0.0017  -0.0049 388 VAL A CG2 
1580 N N   . TRP A 210 ? 0.2726 0.3727 0.2841 0.0100  -0.0028 0.0007  389 TRP A N   
1581 C CA  . TRP A 210 ? 0.2786 0.3755 0.2878 0.0133  -0.0061 0.0050  389 TRP A CA  
1582 C C   . TRP A 210 ? 0.2856 0.3893 0.3012 0.0196  -0.0106 0.0059  389 TRP A C   
1583 O O   . TRP A 210 ? 0.2662 0.3827 0.2873 0.0200  -0.0120 0.0029  389 TRP A O   
1584 C CB  . TRP A 210 ? 0.2780 0.3772 0.2806 0.0088  -0.0063 0.0054  389 TRP A CB  
1585 C CG  . TRP A 210 ? 0.2821 0.3731 0.2795 0.0041  -0.0018 0.0043  389 TRP A CG  
1586 C CD1 . TRP A 210 ? 0.2875 0.3707 0.2803 0.0038  -0.0003 0.0067  389 TRP A CD1 
1587 C CD2 . TRP A 210 ? 0.2843 0.3741 0.2813 -0.0007 0.0016  0.0003  389 TRP A CD2 
1588 N NE1 . TRP A 210 ? 0.2990 0.3771 0.2901 0.0003  0.0039  0.0039  389 TRP A NE1 
1589 C CE2 . TRP A 210 ? 0.2889 0.3694 0.2821 -0.0024 0.0048  0.0004  389 TRP A CE2 
1590 C CE3 . TRP A 210 ? 0.2938 0.3892 0.2935 -0.0041 0.0025  -0.0031 389 TRP A CE3 
1591 C CZ2 . TRP A 210 ? 0.3047 0.3797 0.2974 -0.0062 0.0081  -0.0025 389 TRP A CZ2 
1592 C CZ3 . TRP A 210 ? 0.3073 0.3964 0.3047 -0.0092 0.0059  -0.0052 389 TRP A CZ3 
1593 C CH2 . TRP A 210 ? 0.3111 0.3891 0.3052 -0.0096 0.0084  -0.0048 389 TRP A CH2 
1594 N N   . TYR A 211 ? 0.2895 0.3844 0.3053 0.0244  -0.0129 0.0100  390 TYR A N   
1595 C CA  . TYR A 211 ? 0.2918 0.3895 0.3142 0.0317  -0.0179 0.0118  390 TYR A CA  
1596 C C   . TYR A 211 ? 0.3081 0.4074 0.3256 0.0323  -0.0231 0.0179  390 TYR A C   
1597 O O   . TYR A 211 ? 0.3080 0.4003 0.3161 0.0281  -0.0223 0.0218  390 TYR A O   
1598 C CB  . TYR A 211 ? 0.2909 0.3764 0.3163 0.0363  -0.0176 0.0123  390 TYR A CB  
1599 C CG  . TYR A 211 ? 0.2841 0.3716 0.3143 0.0361  -0.0133 0.0055  390 TYR A CG  
1600 C CD1 . TYR A 211 ? 0.2829 0.3647 0.3080 0.0306  -0.0090 0.0041  390 TYR A CD1 
1601 C CD2 . TYR A 211 ? 0.2786 0.3757 0.3184 0.0411  -0.0137 0.0003  390 TYR A CD2 
1602 C CE1 . TYR A 211 ? 0.2817 0.3660 0.3091 0.0294  -0.0055 -0.0013 390 TYR A CE1 
1603 C CE2 . TYR A 211 ? 0.2752 0.3758 0.3179 0.0398  -0.0091 -0.0063 390 TYR A CE2 
1604 C CZ  . TYR A 211 ? 0.2725 0.3662 0.3077 0.0335  -0.0052 -0.0067 390 TYR A CZ  
1605 O OH  . TYR A 211 ? 0.2831 0.3807 0.3192 0.0314  -0.0012 -0.0126 390 TYR A OH  
1606 N N   . PHE A 212 ? 0.3113 0.4214 0.3357 0.0376  -0.0286 0.0186  391 PHE A N   
1607 C CA  . PHE A 212 ? 0.3338 0.4482 0.3537 0.0383  -0.0350 0.0249  391 PHE A CA  
1608 C C   . PHE A 212 ? 0.3408 0.4436 0.3616 0.0453  -0.0404 0.0324  391 PHE A C   
1609 O O   . PHE A 212 ? 0.3370 0.4352 0.3677 0.0525  -0.0410 0.0308  391 PHE A O   
1610 C CB  . PHE A 212 ? 0.3319 0.4663 0.3600 0.0402  -0.0393 0.0220  391 PHE A CB  
1611 C CG  . PHE A 212 ? 0.3493 0.4955 0.3760 0.0320  -0.0350 0.0152  391 PHE A CG  
1612 C CD1 . PHE A 212 ? 0.3638 0.5076 0.3783 0.0235  -0.0327 0.0153  391 PHE A CD1 
1613 C CD2 . PHE A 212 ? 0.3542 0.5137 0.3921 0.0326  -0.0329 0.0083  391 PHE A CD2 
1614 C CE1 . PHE A 212 ? 0.3746 0.5265 0.3880 0.0159  -0.0288 0.0089  391 PHE A CE1 
1615 C CE2 . PHE A 212 ? 0.3587 0.5273 0.3948 0.0240  -0.0290 0.0027  391 PHE A CE2 
1616 C CZ  . PHE A 212 ? 0.3622 0.5257 0.3861 0.0158  -0.0272 0.0031  391 PHE A CZ  
1617 N N   . ASP A 213 ? 0.3514 0.4490 0.3611 0.0427  -0.0440 0.0405  392 ASP A N   
1618 C CA  . ASP A 213 ? 0.3590 0.4480 0.3686 0.0488  -0.0513 0.0498  392 ASP A CA  
1619 C C   . ASP A 213 ? 0.3613 0.4661 0.3759 0.0536  -0.0598 0.0524  392 ASP A C   
1620 O O   . ASP A 213 ? 0.3458 0.4632 0.3532 0.0477  -0.0612 0.0525  392 ASP A O   
1621 C CB  . ASP A 213 ? 0.3746 0.4509 0.3687 0.0426  -0.0511 0.0581  392 ASP A CB  
1622 C CG  . ASP A 213 ? 0.3806 0.4485 0.3716 0.0475  -0.0598 0.0697  392 ASP A CG  
1623 O OD1 . ASP A 213 ? 0.3799 0.4339 0.3781 0.0542  -0.0617 0.0721  392 ASP A OD1 
1624 O OD2 . ASP A 213 ? 0.3708 0.4456 0.3520 0.0444  -0.0650 0.0762  392 ASP A OD2 
1625 N N   . ALA A 214 ? 0.3709 0.4752 0.3986 0.0645  -0.0655 0.0541  393 ALA A N   
1626 C CA  . ALA A 214 ? 0.3766 0.4978 0.4137 0.0712  -0.0743 0.0561  393 ALA A CA  
1627 C C   . ALA A 214 ? 0.3886 0.5137 0.4119 0.0668  -0.0817 0.0662  393 ALA A C   
1628 O O   . ALA A 214 ? 0.3830 0.5280 0.4067 0.0643  -0.0855 0.0646  393 ALA A O   
1629 C CB  . ALA A 214 ? 0.3690 0.4836 0.4213 0.0845  -0.0794 0.0580  393 ALA A CB  
1630 N N   . ASP A 215 ? 0.4075 0.5139 0.4179 0.0648  -0.0835 0.0762  394 ASP A N   
1631 C CA  . ASP A 215 ? 0.4328 0.5402 0.4280 0.0607  -0.0909 0.0875  394 ASP A CA  
1632 C C   . ASP A 215 ? 0.4227 0.5429 0.4041 0.0483  -0.0863 0.0830  394 ASP A C   
1633 O O   . ASP A 215 ? 0.4017 0.5386 0.3789 0.0460  -0.0927 0.0849  394 ASP A O   
1634 C CB  . ASP A 215 ? 0.4728 0.5560 0.4568 0.0598  -0.0921 0.0988  394 ASP A CB  
1635 C CG  . ASP A 215 ? 0.5000 0.5668 0.4974 0.0717  -0.0959 0.1021  394 ASP A CG  
1636 O OD1 . ASP A 215 ? 0.4793 0.5496 0.4855 0.0816  -0.1063 0.1084  394 ASP A OD1 
1637 O OD2 . ASP A 215 ? 0.5345 0.5855 0.5343 0.0710  -0.0886 0.0979  394 ASP A OD2 
1638 N N   . GLU A 216 ? 0.4218 0.5344 0.3969 0.0406  -0.0755 0.0765  395 GLU A N   
1639 C CA  . GLU A 216 ? 0.4321 0.5526 0.3942 0.0292  -0.0697 0.0714  395 GLU A CA  
1640 C C   . GLU A 216 ? 0.4293 0.5698 0.3995 0.0279  -0.0695 0.0616  395 GLU A C   
1641 O O   . GLU A 216 ? 0.4267 0.5795 0.3874 0.0206  -0.0708 0.0599  395 GLU A O   
1642 C CB  . GLU A 216 ? 0.4434 0.5505 0.4009 0.0235  -0.0587 0.0668  395 GLU A CB  
1643 C CG  . GLU A 216 ? 0.4614 0.5734 0.4052 0.0125  -0.0523 0.0622  395 GLU A CG  
1644 C CD  . GLU A 216 ? 0.4904 0.5920 0.4336 0.0084  -0.0417 0.0564  395 GLU A CD  
1645 O OE1 . GLU A 216 ? 0.5306 0.6187 0.4716 0.0088  -0.0398 0.0618  395 GLU A OE1 
1646 O OE2 . GLU A 216 ? 0.4686 0.5757 0.4140 0.0047  -0.0357 0.0468  395 GLU A OE2 
1647 N N   . ARG A 217 ? 0.4286 0.5723 0.4159 0.0341  -0.0673 0.0548  396 ARG A N   
1648 C CA  . ARG A 217 ? 0.4387 0.6012 0.4358 0.0327  -0.0666 0.0457  396 ARG A CA  
1649 C C   . ARG A 217 ? 0.4339 0.6154 0.4329 0.0346  -0.0772 0.0495  396 ARG A C   
1650 O O   . ARG A 217 ? 0.4330 0.6302 0.4289 0.0272  -0.0774 0.0442  396 ARG A O   
1651 C CB  . ARG A 217 ? 0.4648 0.6270 0.4794 0.0399  -0.0630 0.0395  396 ARG A CB  
1652 C CG  . ARG A 217 ? 0.4987 0.6821 0.5260 0.0394  -0.0628 0.0309  396 ARG A CG  
1653 C CD  . ARG A 217 ? 0.5449 0.7319 0.5671 0.0286  -0.0547 0.0222  396 ARG A CD  
1654 N NE  . ARG A 217 ? 0.5789 0.7837 0.6150 0.0285  -0.0534 0.0144  396 ARG A NE  
1655 C CZ  . ARG A 217 ? 0.5869 0.7970 0.6219 0.0194  -0.0472 0.0067  396 ARG A CZ  
1656 N NH1 . ARG A 217 ? 0.5854 0.7841 0.6067 0.0108  -0.0420 0.0052  396 ARG A NH1 
1657 N NH2 . ARG A 217 ? 0.5559 0.7825 0.6039 0.0191  -0.0460 0.0003  396 ARG A NH2 
1658 N N   . ALA A 218 ? 0.4281 0.6076 0.4325 0.0442  -0.0864 0.0588  397 ALA A N   
1659 C CA  . ALA A 218 ? 0.4513 0.6491 0.4598 0.0481  -0.0983 0.0641  397 ALA A CA  
1660 C C   . ALA A 218 ? 0.4741 0.6767 0.4617 0.0379  -0.1021 0.0693  397 ALA A C   
1661 O O   . ALA A 218 ? 0.4636 0.6873 0.4514 0.0346  -0.1083 0.0678  397 ALA A O   
1662 C CB  . ALA A 218 ? 0.4361 0.6264 0.4547 0.0615  -0.1071 0.0738  397 ALA A CB  
1663 N N   . ARG A 219 ? 0.4957 0.6800 0.4656 0.0324  -0.0981 0.0746  398 ARG A N   
1664 C CA  . ARG A 219 ? 0.5254 0.7128 0.4735 0.0223  -0.1005 0.0794  398 ARG A CA  
1665 C C   . ARG A 219 ? 0.5436 0.7395 0.4841 0.0103  -0.0918 0.0670  398 ARG A C   
1666 O O   . ARG A 219 ? 0.5513 0.7570 0.4764 0.0014  -0.0942 0.0670  398 ARG A O   
1667 C CB  . ARG A 219 ? 0.5329 0.6988 0.4656 0.0201  -0.0984 0.0892  398 ARG A CB  
1668 C CG  . ARG A 219 ? 0.5475 0.7033 0.4837 0.0302  -0.1087 0.1035  398 ARG A CG  
1669 C CD  . ARG A 219 ? 0.5702 0.7063 0.4884 0.0256  -0.1076 0.1147  398 ARG A CD  
1670 N NE  . ARG A 219 ? 0.5976 0.7215 0.5195 0.0353  -0.1180 0.1289  398 ARG A NE  
1671 C CZ  . ARG A 219 ? 0.6117 0.7439 0.5312 0.0396  -0.1318 0.1400  398 ARG A CZ  
1672 N NH1 . ARG A 219 ? 0.6164 0.7707 0.5279 0.0338  -0.1369 0.1386  398 ARG A NH1 
1673 N NH2 . ARG A 219 ? 0.6154 0.7332 0.5406 0.0497  -0.1408 0.1525  398 ARG A NH2 
1674 N N   . ALA A 220 ? 0.5533 0.7445 0.5039 0.0101  -0.0819 0.0565  399 ALA A N   
1675 C CA  . ALA A 220 ? 0.5995 0.7956 0.5453 -0.0001 -0.0735 0.0447  399 ALA A CA  
1676 C C   . ALA A 220 ? 0.6362 0.8551 0.5889 -0.0029 -0.0786 0.0386  399 ALA A C   
1677 O O   . ALA A 220 ? 0.6415 0.8683 0.5841 -0.0133 -0.0765 0.0319  399 ALA A O   
1678 C CB  . ALA A 220 ? 0.5818 0.7649 0.5359 0.0010  -0.0628 0.0375  399 ALA A CB  
1679 N N   . LYS A 221 ? 0.6681 0.8981 0.6390 0.0062  -0.0851 0.0403  400 LYS A N   
1680 C CA  . LYS A 221 ? 0.7106 0.9648 0.6921 0.0042  -0.0899 0.0343  400 LYS A CA  
1681 C C   . LYS A 221 ? 0.7365 1.0073 0.7092 0.0017  -0.1019 0.0407  400 LYS A C   
1682 O O   . LYS A 221 ? 0.7424 1.0304 0.7117 -0.0075 -0.1037 0.0342  400 LYS A O   
1683 C CB  . LYS A 221 ? 0.7023 0.9643 0.7077 0.0150  -0.0915 0.0328  400 LYS A CB  
1684 C CG  . LYS A 221 ? 0.7168 0.9688 0.7309 0.0149  -0.0799 0.0243  400 LYS A CG  
1685 C CD  . LYS A 221 ? 0.7325 0.9891 0.7428 0.0025  -0.0721 0.0133  400 LYS A CD  
1686 C CE  . LYS A 221 ? 0.7247 1.0079 0.7443 -0.0022 -0.0768 0.0076  400 LYS A CE  
1687 N NZ  . LYS A 221 ? 0.7210 1.0184 0.7630 0.0062  -0.0781 0.0055  400 LYS A NZ  
1688 N N   . VAL A 222 ? 0.7723 1.0374 0.7410 0.0093  -0.1104 0.0537  401 VAL A N   
1689 C CA  . VAL A 222 ? 0.8247 1.1046 0.7844 0.0080  -0.1235 0.0623  401 VAL A CA  
1690 C C   . VAL A 222 ? 0.8658 1.1447 0.7997 -0.0067 -0.1203 0.0600  401 VAL A C   
1691 O O   . VAL A 222 ? 0.8705 1.1688 0.7990 -0.0153 -0.1244 0.0549  401 VAL A O   
1692 C CB  . VAL A 222 ? 0.8255 1.0960 0.7864 0.0199  -0.1334 0.0782  401 VAL A CB  
1693 C CG1 . VAL A 222 ? 0.8214 1.1043 0.7681 0.0171  -0.1471 0.0892  401 VAL A CG1 
1694 C CG2 . VAL A 222 ? 0.8152 1.0898 0.8033 0.0350  -0.1375 0.0789  401 VAL A CG2 
1695 N N   . LYS A 223 ? 0.9083 1.1654 0.8269 -0.0098 -0.1125 0.0629  402 LYS A N   
1696 C CA  . LYS A 223 ? 0.9291 1.1839 0.8233 -0.0230 -0.1079 0.0601  402 LYS A CA  
1697 C C   . LYS A 223 ? 0.9250 1.1708 0.8193 -0.0300 -0.0930 0.0455  402 LYS A C   
1698 O O   . LYS A 223 ? 0.9247 1.1808 0.8111 -0.0406 -0.0904 0.0353  402 LYS A O   
1699 C CB  . LYS A 223 ? 0.9459 1.1847 0.8231 -0.0227 -0.1088 0.0728  402 LYS A CB  
1700 C CG  . LYS A 223 ? 0.9470 1.1898 0.7969 -0.0359 -0.1080 0.0731  402 LYS A CG  
1701 C CD  . LYS A 223 ? 0.9439 1.1703 0.7766 -0.0374 -0.1065 0.0849  402 LYS A CD  
1702 C CE  . LYS A 223 ? 0.9425 1.1516 0.7712 -0.0416 -0.0908 0.0775  402 LYS A CE  
1703 N NZ  . LYS A 223 ? 0.9462 1.1425 0.7970 -0.0319 -0.0848 0.0738  402 LYS A NZ  
# 
